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| Product | Description | |
|---|---|---|
| 6-Nitroveratraldehyde | DMNB is a derivative of vanillin with 100-fold potency compared to vanillin, and acts as an inhibitor of DNA-dependent protein kinase (DNA-PK) (IC50 = 15 μM). DNA-PK is an enzyme involved in the non-homologous end-joining (NHEJ) pathway of double-stranded DNA break (DSB) repair in human cells. Uses: Dmnb is a vanillin compound, which is a type of dna-pk inhibitor. Synonyms: 4,5-dimethoxy-2-nitrobenzaldehyde. Grades: ≥ 98 % by HPLC. CAS No. 20357-25-9. Molecular formula: C9H9NO5. Mole weight: 211.17. |  |
| acetoacetyl-CoA synthase | The enzyme from the soil bacterium Streptomyces sp. CL190 produces acetoacetyl-CoA to be used for mevalonate production via the mevalonate pathway.Unlike the homologous EC 2.3.1.180 (β-ketoacyl-[acyl-carrier-protein] synthase III), this enzyme does not accept malonyl-[acyl-carrier-protein] as a substrate. Group: Enzymes. Synonyms: NphT7. Enzyme Commission Number: EC 2.3.1.194. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2137; acetoacetyl-CoA synthase; EC 2.3.1.194; NphT7. Cat No: EXWM-2137. |  |
| AminoAcylase-1 from Human, Recombinant | Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes. Acy1 recombinant human produced in e. coli is a single, non-... SDS-PAGE. ACY1. Mole weight: 48 kDa. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. N-acyl-L-amino-acid amidohydrolase; ACY-1, ACY1D; ACYLASE; ACY1; aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short | |
| caspase-8 | Caspase-8 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Caspase-8 is the apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. It contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. This enzyme is linked to cell surface death receptors such as Fas. When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. The enzyme has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala, at the P1' position. It has very broad P...ORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Enzyme Commission Number: EC 3.4.22.61. CAS No. 179241-78-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4237; caspase-8; EC 3.4.22.61; 179241-78-2; FLICE, FADD-like ICE; MACH; MORT1-associated CED-3 homolog; Mch5; mammalian Ced-3 homolog 5; CASP-8; ICE-like apoptotic protease 5; FADD-homologous ICE/CED-3-like protease; apoptotic cysteine protease; apoptotic protease Mch-5; CAP4. Cat No: EXWM-4237. | |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| GDP-mannose 4,6-dehydratase | The bacterial enzyme requires bound NAD+. This enzyme forms the first step in the biosynthesis of GDP-α-D-rhamnose and GDP-β-L-fucose. In Aneurinibacillus thermoaerophilus L420-91T, this enzyme acts as a bifunctional enzyme, catalysing the above reaction as well as the reaction catalysed by EC 1.1.1.281, GDP-4-dehydro-6-deoxy-D-mannose reductase. Belongs to the short-chain dehydrogenase/reductase enzyme family, having homologous structures and a conserved catalytic triad of Lys, Tyr and Ser/Thr residues. Group: Enzymes. Synonyms: guanosine 5'-diphosphate-D-mannose oxidoreductase; guanosine diphosphomannose oxidoreductase; guanosine diphosphomannose 4,6-dehydratase; GDP-D-mannose dehydratase; GDP-D-mannose 4,6-dehydratase; Gmd; GDP-mannose 4,6-hydro-lyase; GDP-mannose 4,6-hydro-. Enzyme Commission Number: EC 4.2.1.47. CAS No. 37211-59-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5036; GDP-mannose 4,6-dehydratase; EC 4.2.1.47; 37211-59-9; guanosine 5'-diphosphate-D-mannose oxidoreductase; guanosine diphosphomannose oxidoreductase; guanosine diphosphomannose 4,6-dehydratase; GDP-D-mannose dehydratase; GDP-D-mannose 4,6-dehydratase; Gmd; GDP-mannose 4,6-hydro-lyase; GDP-mannose 4,6-hydro-lyase (GDP-4-dehydro-6-deoxy-D-mannose-forming). Cat No: EXWM-5036. | |
| Histidyl-tRNA Synthetase from Human, Recombinant | Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis. Histidyl-trna synthetase human recombinant produced in...thetase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Histidyl-tRNA synthetase; EC 6.1.1.21; Histidine-tRNA ligase; HisRS; HRS; FLJ20491; JO-1. Enzyme Commission Number: EC 6.1.1.21. CAS No. 9068-78-4. Purity: Greater than 90.0% as determined by both (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. HRS. Stability: Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Histidyl-tRNA synthetase; EC 6.1.1.21; Histidine-tRNA ligase; HisRS; HRS; FLJ20491; JO-1. Cat No: NATE-0848. | |
| mitochondrial processing peptidase | Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin, and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Enzyme Commission Number: EC 3.4.24.64. CAS No. 86280-61-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4347; mitochondrial processing peptidase; EC 3.4.24.64; 86280-61-7; processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Cat No: EXWM-4347. | |
| ML216 | Bloom (BLM) helicase is a DNA unwinding enzyme important for DNA repair in the homologous recombination pathway. Mutations of the BLM gene result in reduced BLM helicase activity that is associated with the rare genetic disorder, Bloom's Syndrome, and a predisposition to developing cancer. ML-216 is the first identified small molecule inhibitor of BLM helicase (IC50 = 1.8 μM) that is 28-fold selective against the related helicases RECQ1, RECQ5, and E. coli UvrD (IC50s ≥ 50 μM). At 25-50 μM, ML-216 has been shown to dose-dependently inhibit the proliferation of BLM-expressing PSNF5 fibroblast cells but not BLM-deficient PSNG13 fibroblast cells. Synonyms: ML 216; ML-216; CID-49852229; CID49852229; CID 49852229. Grades: >98%. CAS No. 1430213-30-1. Molecular formula: C15H9F4N5OS. Mole weight: 383.32. | |
| molybdenum cofactor sulfurtransferase | Contains pyridoxal phosphate. Replaces the equatorial oxo ligand of the molybdenum by sulfur via an enzyme-bound persulfide. The reaction occurs in prokaryotes and eukaryotes but MoCo sulfurtransferases are only found in eukaryotes. In prokaryotes the reaction is catalysed by two enzymes: cysteine desulfurase (EC 2.8.1.7), which is homologous to the N-terminus of eukaryotic MoCo sulfurtransferases, and a molybdo-enzyme specific chaperone which binds the MoCo and acts as an adapter protein. Group: Enzymes. Synonyms: molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase. Enzyme Commission Number: EC 2.8.1.9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3367; molybdenum cofactor sulfurtransferase; EC 2.8.1.9; molybdenum cofactor sulfurase; ABA3; HMCS; MoCo sulfurase; MoCo sulfurtransferase. Cat No: EXWM-3367. | |
| Native Human Calpain 1 | Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneRation, and autoimmune demyelinating diseases such as multiple sclerosis. > 95% (sds-page). Applications: Human calpain 1 has been used in a study to assess how the crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. human calpain 1 has also been used in a study to investigate the synthesis, biological evaluation and molecular modelling of n-heterocyclic dipeptide aldehydes as selective calpain inhibitors. Group: Enzymes. Synonyms: calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Enzyme Commission Number: EC 3.4.22.52. CAS No. 78990-62-2. Calpain 1. Storage: -70°C. Form: aqueous glycerol solution. Source: Human. calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Cat No: NATE-0100. | |
| Native Porcine Calpain 1 | Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneRation, and autoimmune demyelinating diseases such as multiple sclerosis. Group: Enzymes. Synonyms: μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Purity: > = 95% by SDS-PAGE. Calpain 1. Mole weight: 110000. Stability: > 1 year. Storage: -70°C or lower; avoid freeze/thaw cycles. Form: Frozen. Source: Porcine Erythrocytes. Species: Porcine. calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Cat No: NATE-1625. | |
| PDD 00017273 | PDD 00017273 is a potent and selective poly (ADP ribose) glycohydrolase (PARG) inhibitor (IC50 = 26 nM), with >350-fold selectivity for PARG over a panel of ion channels, enzymes and receptors, including PARP1 and ARH3. PARG has been shown to be involved in the repair of single strand DNA breaks. PDD 00017273 (0.3 μM) also reduces the viability of BRCA1, BRCA2, PALB2, FAM175A, and BARD1 depleted cells. PDD 00017273 stalls replication forks and induces DNA damage that requires homologous recombination (HR) for repair. Synonyms: 1-[(1,3-Dimethyl-1H-pyrazol-5-yl)methyl]-1,2,3,4-tetrahydro-N-(1-methylcyclopropyl)-3-[(2-methyl-5-thiazolyl)methyl]-2,4-dioxo-6-quinazolinesulfonamide. Grades: ≥98% by HPLC. CAS No. 1945950-21-9. Molecular formula: C23H26N6O4S2. Mole weight: 514.62. | |
| picornain 2A | From entero-, rhino-, aphto- and cardioviruses. Smaller than the homologous picornain 3C, which is also in peptidase family C3 (picornain 3C family). Group: Enzymes. Synonyms: picornavirus endopeptidase 2A; poliovirus protease 2A; rhinovirus protease 2A; 2A protease; 2A proteinase; protease 2A; proteinase 2Apro; picornaviral 2A proteinase; Y-G proteinase 2A; poliovirus proteinase 2A; poliovirus protease 2Apro; picornaviral 2A proteinase. Enzyme Commission Number: EC 3.4.22.29. CAS No. 103406-62-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4203; picornain 2A; EC 3.4.22.29; 103406-62-8; picornavirus endopeptidase 2A; poliovirus protease 2A; rhinovirus protease 2A; 2A protease; 2A proteinase; protease 2A; proteinase 2Apro; picornaviral 2A proteinase; Y-G proteinase 2A; poliovirus proteinase 2A; poliovirus protease 2Apro; picornaviral 2A proteinase. Cat No: EXWM-4203. | |
| picornain 3C | From entero-, rhino-, aphto- and cardioviruses. Larger than the homologous virus picornain 2A. Type example of peptidase family C3. Group: Enzymes. Synonyms: picornavirus endopeptidase 3C; poliovirus protease 3C; rhinovirus protease 3C; foot-and-mouth protease 3C; poliovirus proteinase 3C; rhinovirus proteinase 3C; coxsackievirus 3C proteinase; foot-and-mouth-disease virus proteinase 3C; 3C protease; 3C proteinase; cysteine proteinase 3C; hepatitis A virus 3C proteinase; protease 3C; tomato ringspot nepovirus 3C-related protease. Enzyme Commission Number: EC 3.4.22.28. CAS No. 97162-88-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4202; picornain 3C; EC 3.4.22.28; 97162-88-4; picornavirus endopeptidase 3C; poliovirus protease 3C; rhinovirus protease 3C; foot-and-mouth protease 3C; poliovirus proteinase 3C; rhinovirus proteinase 3C; coxsackievirus 3C proteinase; foot-and-mouth-disease virus proteinase 3C; 3C protease; 3C proteinase; cysteine proteinase 3C; hepatitis A virus 3C proteinase; protease 3C; tomato ringspot nepovirus 3C-related protease. Cat No: EXWM-4202. | |
| sphingolipid 8-(E)-desaturase | The enzyme, characterized from the yeasts Kluyveromyces lactis and Candida albicans and from the diatom Thalassiosira pseudonana, introduces a trans double bond at the 8-position of sphingoid bases in sphingolipids. The enzyme determines the position of the double bond by its distance from the alcohol end of the sphingoid base, and contains a cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase. The homologous enzymes from higher plants, EC 1.14.19.29, sphingolipid 8-(E/Z)-desaturase, act on phytosphinganine (4-hydroxysphinganine) and produces a mixture of trans and cis isomers. Group: Enzymes. Synonyms: 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.18. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0980; sphingolipid 8-(E)-desaturase; EC 1.14.19.18; 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Cat No: EXWM-0980. | |
| sphingolipid 8-(E/Z)-desaturase | The enzymes from higher plants convert sphinganine, 4E-sphing-4-enine and phytosphinganine into E/Z-mixtures of Δ8-desaturated products displaying different proportions of geometrical isomers depending on plant species. The nature of the actual desaturase substrate has not yet been studied experimentally. The enzymes contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the active site of the desaturase. The homologous enzymes from some yeasts and diatoms, EC 1.14.19.18, sphingolipid 8-(E)-desaturase, act on sphing-4-enine ceramides and produce only the trans isomer. Group: Enzymes. Synonyms: 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Enzyme Commission Number: EC 1.14.19.29. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0992; sphingolipid 8-(E/Z)-desaturase; EC 1.14.19.29; 8-sphingolipid desaturase (ambiguous); 8 fatty acid desaturase (ambiguous); DELTA8-sphingolipid desaturase (ambiguous). Cat No: EXWM-0992. | |
| stromelysin 1 | An extracellular endopeptidase of vertebrate tissues homologous with interstitial collagenase. Digests proteoglycan, fibronectin, collagen types III, IV, V, IX, and activates procollagenase. In peptidase family M10 (interstitial collagenase family). Group: Enzymes. Synonyms: matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Enzyme Commission Number: EC 3.4.24.17. CAS No. 79955-99-0. Matrix Metalloproteinase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4298; stromelysin 1; EC 3.4.24.17; 79955-99-0; matrix metalloproteinase 3; proteoglycanase; collagenase activating protein; procollagenase activator; transin; MMP-3; neutral proteoglycanase; stromelysin; collagen-activating protein. Cat No: EXWM-4298. | |
| subtilisin | Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. Group: Enzymes. Synonyms: alcalase; alcala. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9014-1-1. Protease. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4153; subtilisin; EC 3.4.21.62; 9014-01-1; alcalase; alcalase 0.6L; alcalase 2.5L; ALK-enzyme; bacillopeptidase A; bacillopeptidase B; Bacillus subtilis alkaline proteinase bioprase; bioprase AL 15; bioprase APL 30; colistinase; (see also comments); subtilisin J; subtilisin S41; subtilisin Sendai; subtilisin GX; subtilisin E; subtilisin BL; genenase I; esperase; maxatase; alcalase; thermoase PC 10; protease XXVII; thermoase; superase; subtilisin DY; subtilopeptidase; SP 266; savinase 8.0L; savinase 4.0T; kazusase; protease VIII; opticlean; Bacillus subtilis alkaline proteinase; protin A 3L; savinase; savinase 16.0L; savinase 32.0 L EX | |
| tRNase Z | No cofactor requirements. An homologous enzyme to that found in Arabidopsis thaliana has been found in Methanococcus janaschii. Group: Enzymes. Synonyms: 3 tRNase; tRNA 3 endonuclease; RNase Z; 3' tRNase. Enzyme Commission Number: EC 3.1.26.11. CAS No. 98148-84-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3587; tRNase Z; EC 3.1.26.11; 98148-84-6; 3 tRNase; tRNA 3 endonuclease; RNase Z; 3' tRNase. Cat No: EXWM-3587. | |
| yapsin 1 | In peptidase family A1 of pepsin, and weakly inhibited by pepstatin. Can partially substitute for kexin in a deficient strain of yeast. The homologous product of the Mkc7 gene (Saccharomyces cerevisiae) has similar catalytic activity and has been termed yapsin 2. Group: Enzymes. Synonyms: yeast aspartic protease 3; Yap3 gene product (Saccharomyces cerevisiae). Enzyme Commission Number: EC 3.4.23.41. CAS No. 205132-58-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4278; yapsin 1; EC 3.4.23.41; 205132-58-7; yeast aspartic protease 3; Yap3 gene product (Saccharomyces cerevisiae). Cat No: EXWM-4278. | |
| 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanol Sodium Salt | Phosphatidylethanol (PEth) represents a group of glycerophospholipid homologues generated by substitution of ethanol for the lipid headgroup by the phospholipase D enzyme. Since the formation of PEth is specifically dependent on ethanol, the diagnostic specificity of PEth as an alcohol biomarker is theoretically 100%. Group: Biochemicals. Grades: Highly Purified. CAS No. 322647-55-2. Pack Sizes: 1mg, 5mg. Molecular Formula: C39H74NaO8P, Molecular Weight: 724.96. US Biological Life Sciences. |  Worldwide |
| 2-amino-4-deoxychorismate synthase | Requires Mg2+. The reaction occurs in the reverse direction to that shown above. In contrast to most anthranilate-synthase I (ASI) homologues, this enzyme is not inhibited by tryptophan. In Streptomyces globisporus, the sequential action of this enzyme and EC 1.3.99.24, 2-amino-4-deoxychorismate dehydrogenase, leads to the formation of the benzoxazolinate moiety of the enediyne antitumour antibiotic C-1027.In certain Pseudomonads the enzyme participates in the biosynthesis of phenazine, a precursor for several compounds with antibiotic activity. Group: Enzymes. Synonyms: ADIC synthase; 2-amino-2-deoxyisochorismate synthase;SgcD. Enzyme Commission Number: EC 2.6.1.86. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2927; 2-amino-4-deoxychorismate synthase; EC 2.6.1.86; ADIC synthase; 2-amino-2-deoxyisochorismate synthase;SgcD. Cat No: EXWM-2927. | |
| Abl Kinase Mutant active human, Recombinant | Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9. c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene. Human abelson murine leukemia viral oncogene homolog 1 (abl-1) (genbank accession no. nm_007313), amino acids 248-531 with t334i mutation and n-terminal his-tag, mw = 33 kda, expressed in a baculovirus-infected sf9 cell expression system. Group: Enzymes. Synonyms: ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Abl Kinase. Mole weight: mol wt 33 kDa. Stability: -70°C. Form: aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Cat No: NATE-0013. | |
| α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277. | |
| α(2-3) Neuraminidase from Salmonella typhimurium LT2, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Α2-3 neuraminidase is a highly specific exogl... sialyl linkages and shows only trace activity against α2-8 sialyl linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Neuraminidase. Mole weight: 41 kDa. Activity: ~11,300,000 units/mg. Storage: Store at 4°C or in small aliquots at -20°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), and 5 mM Na2EDTA. Source: E. coli. Species: Salmonella typhimurium LT2. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase. Cat No: NATE-1276. | |
| α(2-3) Neuraminidase S from Streptococcus pneumoniae, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neurami...;2-3 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 74000 daltons. Activity: 160,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM EDTA. Source: E. coli. Species: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase S; α(2-3) Neuraminidase. Cat No: NATE-1275. | |
| Angiotensin Fragment 1-7 acetate | Angiotensin Fragment 1-7 is a major active component of the renin-angiotensin system (RAS), produced from cleavage of Ang II by angiotensin-converting-enzyme type 2 (ACE2). Angiotensin 1-7 inhibits purified canine ACE activity with IC50 of 0.65 μM. This peptide can be generated by the action of ACE2, a homolog of ACE, on angiotensin II or by the action of neprilysin on angiotensin I. It has been studied in the context of ameliorating the symptoms of metabolic syndrome. Synonyms: 5-L-isoleucine-1-7-angiotensin II; Ang-(1-7). Grades: ≥95%. Molecular formula: C41H62N12O11·xC2H4O2. Mole weight: 899. | |
| archaeosine synthase | In Euryarchaeota the reaction is catalysed by ArcS. In Crenarchaeota, which do not have an ArcS homologue, the reaction is catalysed either by a homologue of EC 6.3.4.20, 7-cyano-7-deazaguanine synthase that includes a glutaminase domain (cf. EC 3.5.1.2), or by a homologue of EC 1.7.1.13, preQ1 synthase. The enzyme from the Euryarchaeon Methanocaldococcus jannaschii can also use arginine and ammonium as amino donors. Group: Enzymes. Synonyms: ArcS; TgtA2; MJ1022 (gene name); glutamine:preQ0-tRNA amidinotransferase (incorrect). Enzyme Commission Number: EC 2.6.1.97. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2938; archaeosine synthase; EC 2.6.1.97; ArcS; TgtA2; MJ1022 (gene name); glutamine:preQ0-tRNA amidinotransferase (incorrect). Cat No: EXWM-2938. | |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile filtered colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. | |
| atrolysin C | A 24 kDa hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox) that digests type IV collagen, and exists as two forms, c and d. Phosphoramidon inhibits in the 0.1 mM range. In peptidase family M12 (astacin family). Hemorrhagic toxin-2 of C. ruber ruber has the same Mr and specificity and is a homologue. Group: Enzymes. Synonyms: Crotalus atrox metalloendopeptidase c; hemorrhagic toxin c and d. Enzyme Commission Number: EC 3.4.24.42. CAS No. 158886-17-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4324; atrolysin C; EC 3.4.24.42; 158886-17-0; Crotalus atrox metalloendopeptidase c; hemorrhagic toxin c and d. Cat No: EXWM-4324. | |
| aureusidin synthase | A copper-containing glycoprotein that plays a key role in the yellow coloration of flowers such as Antirrhinum majus (snapdragon). The enzyme is a homologue of plant polyphenol oxidase and catalyses two separate chemical transformations, i.e. 3-hydroxylation and oxidative cyclization (2',-dehydrogenation). H2O2 activates reaction (1) but inhibits reaction (2). Originally considered to act on the phenol but now thought to act mainly on the 4'-O-β-D-glucoside in vivo. Group: Enzymes. Synonyms: AmAS1. Enzyme Commission Number: EC 1.21.3.6. CAS No. 320784-48-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1253; aureusidin synthase; EC 1.21.3.6; 320784-48-3; AmAS1. Cat No: EXWM-1253. | |
| Beetroot Powder | Beet root powder is an excellent source of folate and a good source of manganese, and contains betaines which may function to reduce the concentration of homocysteine, a homolog of the naturally occurring amino acid cysteine. Beetroot powder is rich in nutrients, offers various health benefits. Apart from the health benefits, Beet root powder is found to be used as food colorants and as a traditional home remedy. The following are some of the health benefits of beetroot. Beetroot powder benefits for skin includes its cleansing action, which helps in eliminating toxins from the body. Group: Others. Beetroot Powder; Beta Vulgaris. Cat No: EXTC-103. | |
| Bovine factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig... activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. CAS No. 9001-28-9. Purity: >95% by SDS-PAGE. Factor IX. Mole weight: 55400. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine factor IX; Factor IX. Pack: 100 ug. Cat No: CZY-003. | |
| Bovine Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fa...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Bovine glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...hich remain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine glu-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-015. | |
| Bovine Protein C | The vitamin K-dependent zymogen, protein C, is synthesized in the liver as a single chain polypeptide and is subsequently converted to a disulfide linked heterodimer, by removal of a dipeptide (Lys-146 and Arg-147) from the precursor molecule. Trace quantities of the single chain form have been observed in plasma. The light chain, which is responsible for the calcium dependent binding of protein C to phospholipid vesicles, contains 11 γ-carboxyglutamic acid (gla) residues, 1 b-hydroxyaspartic acid residue, and 2 epidermal growth factor (EGF) homology domains. The serine protease catalytic triad is located in the heavy chain. Human protein C is susceptible to proteolytic cleavag...g the proteolytic inactivation of factors Va and VIIIa. APC also contributes to the fibrinolytic response by complex formation with plasminogen activator inhibitors.Bovine protein C is prepared from fresh citrated bovine plasma by a modification of the Walker procedure, as described by Haley et al. Human protein C is prepared from fresh frozen citrated human plasma using a combination of immunoaffinity chromatography, and conventional techniques. Protein C is provided in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a chromogenic substrate based assay. Group: Zymogens. Purity: >95% by SDS-PAGE. Prote | |
| Bovine Prothrombin | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature p...Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| CGM097 | CGM097 is an orally bioavailable HDM2 (human homolog of double minute 2) antagonist with potential antineoplastic activity. Upon oral administration, p53/HDM2 interaction inhibitor CGM097 inhibits the binding of the HDM2 protein to the transcriptional activation domain of the tumor suppressor protein p53. By preventing this HDM2-p53 interaction, the proteosome-mediated enzymatic degradation of p53 is inhibited, which may result in the restoration of p53 signaling and, thus, the p53-mediated induction of tumor cell apoptosis. HDM2, a zinc finger nuclear phosphoprotein, is a negative regulator of the p53 pathway, often overexpressed in cancer cells and has been implicated in cancer cell proliferation and survival. Synonyms: CGM097; CGM-097; CGM 097; NVPCGM097; NVPCGM 097; NVPCGM-097; NVP CGM097; NVP CGM 097; NVP CGM-097. CAS No. 1313363-54-0. Molecular formula: C38H47ClN4O4. Mole weight: 659.27. | |
| coagulation factor IXa | A chymotrypsin homologue, and one of the γ-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Enzyme Commission Number: EC 3.4.21.22. CAS No. 37316-87-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4122; coagulation factor IXa; EC 3.4.21.22; 37316-87-3; activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Cat No: EXWM-4122. | |
| Dipeptidyl Peptidase IV from Human, Recombinant | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contai...zyme from creative enzymes has been used to study the lc-ms (liquid chromatography-mass spectrometry) based assay method for dpp-iv inhibitor screening and substrate discovery. Group: Enzymes. Synonyms: EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidy | |
| Dipeptidyl Peptidase VII from Human, Recombinant | DPP7 is essential for maintaining lymphocytes and fibroblasts in G (0). The inhibition of DPP7 results in apoptosis, which is mediated by the induction of c-Myc and p53. DPP7 has strong sequence homology with prolylcarboxypeptidase and is active at both acidic and neutral pH. Contains amino acids 29 to end with a c-terminal his tag, mw=89.1 kda. Applications: Dipeptidyl peptidase vii (dpp7), also known as dpp2 or quiescent cell proline dipeptidase, is a post-proline cleaving aminopeptidase that is expressed in quiescent lymph ocytes. dpp7 is used to study the regulation of cell quiescence. like dpp4, dpp7 may be useful in diabetes and vascular disease research. Group: Enzymes. Synonyms: EC 3.4.14.-; DPP7; Quiescent cell proline dipeptidase; Dipeptidyl Peptidase VII; DPP VII. Enzyme Commission Number: EC 3.4.14.-. DPP VII. Mole weight: 89.1 kDa. Storage: -70°C. Form: Supplied as a solution in 25 mM Tris-HCl, pH 8.0, 130 mM NaCl, 0.05% Tween-20, 10% glycerol. Source: Sf9 cells. Species: Human. EC 3.4.14.-; DPP7; Quiescent cell proline dipeptidase; Dipeptidyl Peptidase VII; DPP VII. Cat No: NATE-0206. | |
| EPZ011989 | EPZ011989 is a potent, orally-available EZH2 inhibitor with robust in vivo activity. EPZ011989 demonstrates significant tumor growth inhibition in a mouse xenograft model of human B cell lymphoma. EPZ011989 represents a powerful tool for the expanded exploration of EZH2 activity in biology. Inhibitors of the protein methyltransferase Enhancer of Zeste Homolog 2 (EZH2) may have significant therapeutic potential for the treatment of B cell lymphomas and other cancer indications. The ability of the scientific community to explore fully the spectrum of EZH2-associated pathobiology has been hampered by the lack of in vivo-active tool compounds for this enzyme. Group: Inhibitors. Alternative Names: EPZ011989; EPZ-011989; EPZ 011989. CAS No. 1598383-40-4. Molecular formula: C35H51N5O4. Mole weight: 605.82. Appearance: Solid powder. Purity: >98%. IUPACName: N- ( (4, 6-dimethyl-2-oxo-1, 2-dihydropyridin-3-yl)methyl)-3- (ethyl ( (1r, 4r)-4- ( (2-methoxyethyl) (methyl)amino)cyclohexyl)amino)-2-methyl-5- (3-morpholinoprop-1-yn-1-yl)benzamide. Canonical SMILES: O=C (NCC1=C (C)C=C (C)NC1=O)C2=CC (C#CCN3CCOCC3)=CC (N (CC)[C@H]4CC[C@H] (N (CCOC)C)CC4)=C2C. Catalog: ACM1598383404. |  |
| fatty-acid peroxygenase | A cytosolic heme-thiolate protein with sequence homology to P-450 monooxygenases. Unlike the latter, it needs neither NAD(P)H, dioxygen nor specific reductases for function. Enzymes of this type are produced by bacteria (e.g. Sphingomonas paucimobilis, Bacillus subtilis). Catalytic turnover rates are high compared with those of monooxygenation reactions as well as peroxide shunt reactions catalysed by the common P-450s. A model substrate is myristate, but other saturated and unsaturated fatty acids are also hydroxylated. Oxidizes the peroxidase substrate 3,3',5,5'-tetramethylbenzidine (TMB) and peroxygenates aromatic substrates in a fatty-acid-dependent reaction. Group: Enzymes. Synonyms: fatty acid hydroxylase (ambiguous); P450 peroxygenase; CYP152A1; P450BS; P450SP&alpha. Enzyme Commission Number: EC 1.11.2.4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0515; fatty-acid peroxygenase; EC 1.11.2.4; fatty acid hydroxylase (ambiguous); P450 peroxygenase; CYP152A1; P450BS; P450SP&alpha. Cat No: EXWM-0515. | |
| glycyl endopeptidase | From the papaya plant, Carica papaya. Not inhibited by chicken cystatin, unlike most other homologues of papain, but in peptidase family C1 (papain family). Group: Enzymes. Synonyms: papaya peptidase B; papaya proteinase IV; glycine-specific proteinase; chymopapain; Papaya proteinase 4; PPIV; chymopapain M. Enzyme Commission Number: EC 3.4.22.25. CAS No. 149719-24-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4199; glycyl endopeptidase; EC 3.4.22.25; 149719-24-4; papaya peptidase B; papaya proteinase IV; glycine-specific proteinase; chymopapain; Papaya proteinase 4; PPIV; chymopapain M. Cat No: EXWM-4199. | |
| Human Coagulation Factor VII | Human factor VII is a single chain, vitamin K-dependent, plasma glycoprotein which is synthesized in the liver. Prior to secretion into the blood, post translational modification by a vitamin K-dependent carboxylase produces ten-carboxyglutamic acid (gla) residues located in the NH2-terminal portion of the molecule, which facilitate cell membrane binding. Factor VII is proteolytically activated to the serine protease, factor VIIa, during coagulation. Factor VII can be activated by thrombin, factor IXa, factor Xa or factor XIIa. The activation results in cleavage of the single chain molecule on the COOH-terminal side of arginine-152, to produce an NH2-terminal derived light chai...nzyme complex catalyzes the conversion of both factor IX to factor IXa and factor X to factor Xa. The cDNA for factor VII has been isolated and the nucleotide sequence determined. Factor VII shares extensive sequence homology with other serine proteases including factor IX, factor X and protein C.Human factor VII is purified using a combination of conventional techniques and immunoaffinity chromatography. The purified protein is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured in a factor VII clotting assay. Group: Zymogens. CAS No. 9001-25-6. Purity: >95% by SDS-PAGE. Factor VII. Mole weigh | |
| Human Factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig...lly activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. CAS No. 9001-28-9. Purity: >95% by SDS-PAGE. Factor IX. Mole weight: 55000. Stability: 12 months. Storage: -20°C. Source: Human. Human Factor IX; Factor IX. Pack: 100 ug. Cat No: CZY-002. | |
| Human Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fac...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Human gla-domainless Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor ...e prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Human glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p... a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. CAS No. 9001-91-6. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 88000. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-011. | |
| Human glu-Plasminogen CHOI | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of...remain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen CHOI; Plasminogen. Pack: 1 mg. Cat No: CZY-012. | |
| Human glu-Plasminogen CHOII | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction o...emain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Human. Human glu-Plasminogen CHOII; Plasminogen. Pack: 1 mg. Cat No: CZY-013. | |
| Human lys-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...ently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 83000. Stability: 12 months. Storage: -20°C. Source: Human. Human lys-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-014. | |
| Human Prethrombin-1 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature ...Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prethrombin-2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature ...Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Protein C | The vitamin K-dependent zymogen, protein C, is synthesized in the liver as a single chain polypeptide and is subsequently converted to a disulfide linked heterodimer, by removal of a dipeptide (Lys-146 and Arg-147) from the precursor molecule. Trace quantities of the single chain form have been observed in plasma. The light chain, which is responsible for the calcium dependent binding of protein C to phospholipid vesicles, contains 11 γ-carboxyglutamic acid (gla) residues, 1 b-hydroxyaspartic acid residue, and 2 epidermal growth factor (EGF) homology domains. The serine protease catalytic triad is located in the heavy chain. Human protein C is susceptible to proteolytic cleavag...ng the proteolytic inactivation of factors Va and VIIIa. APC also contributes to the fibrinolytic response by complex formation with plasminogen activator inhibitors.Bovine protein C is prepared from fresh citrated bovine plasma by a modification of the Walker procedure, as described by Haley et al. Human protein C is prepared from fresh frozen citrated human plasma using a combination of immunoaffinity chromatography, and conventional techniques. Protein C is provided in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a chromogenic substrate based assay. Group: Zymogens. CAS No. 42617-41-4. Purity: >95 | |
| Human Prothrombin | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature p...-Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 1 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mat...1 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 1.2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the ma... (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| Human Prothrombin Fragment 2 | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mat...1 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| matriptase | This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. The enzyme can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active α- and β-HGF, but It does not activate plasminogen, which shares high homology with HGF.The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Enzyme Commission Number: EC 3.4.21.109. CAS No. 241475-96-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4104; matriptase; EC 3.4.21.109; 241475-96-7; serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Cat No: EXWM-4104. | |
| menaquinol oxidase (H+-transporting) | Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force. Group: Enzymes. Synonyms: cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting). Enzyme Commission Number: EC 7.1.1.5 (Formerly EC 1.10.3.12). Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0478; menaquinol oxidase (H+-transporting); EC 1.10.3.12; cytochrome aa3-600 oxidase; cytochrome bd oxidase; menaquinol:O2 oxidoreductase (H+-transporting). Cat No: EXWM-0478. | |
| Menaquinone 7 | Menaquinone 7 belongs to a class of K2-vitamin homologs originally discovered as the anti-hemorrhagic factors. Menaquinone 7 has been identified as the most bioactive cofactor for the carboxylation reaction of Gla-proteins, such as osteocalcin and matrix-Gla protein, which plays a crucial role in building and maintaining overall bone health. Applications: A bioactive cofactor for the carboxylation reaction of gla-proteins. Group: Coenzymes. Synonyms: (all-E)-2-(3,7,11,15,19,23,27-Heptamethyl-2,6,10,14,18,22,26-octacosaheptaenyl)-3-methyl-1,4-naphthalenedione; Vitamin K2(35); Menaquinone K7. CAS No. 2124-57-4. Purity: ≥90%. Mole weight: 649. Form: Solid. (all-E)-2-(3,7,11,15,19,23,27-Heptamethyl-2,6,10,14,18,22,26-octacosaheptaenyl)-3-methyl-1,4-naphthalenedione; Vitamin K2(35); Menaquinone K7; Menaquinone 7; 2124-57-4. Cat No: COEC-093. | |
| mitochondrial intermediate peptidase | A homologue of thimet oligopeptidase. Natural substrates are precursor proteins that have already been processed by mitochondrial processing peptidase. In peptidase family M3 (thimet oligopeptidase family). Group: Enzymes. Synonyms: mitochondrial intermediate precursor-processing proteinase; MIP. Enzyme Commission Number: EC 3.4.24.59. CAS No. 136447-30-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4341; mitochondrial intermediate peptidase; EC 3.4.24.59; 136447-30-8; mitochondrial intermediate precursor-processing proteinase; MIP. Cat No: EXWM-4341. | |
| Monoglyceride lipase from Human, Recombinant | In enzymology, an acylglycerol lipase (EC 3.1.1.23) is an enzyme that catalyzes a chemical reaction that uses water molecules to break the glycerol monoesters of long-chain fatty acids. This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This enzyme participates in glycerolipid metabolism. Group: Enzymes. Synonyms: MLL; HU-K5; HUK5; MAGL; MGL; Lysophospholipase homolog; Lysophospholipase-like. Enzyme Commission Number: EC 3.1.1.23. Purity: > 85% by SDS-PAGE. Monoglyceride lipase. Mole weight: 36.4 kDa. Activity: > 170 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at N-terminus. Species: Human. acylglycerol lipase; glycerol-ester acylhydrolase; monoacylglycerol lipase; monoacylglycerolipase; monoglyceride lipase; monoglyceride hydrolase; fatty acyl monoester lipase; monoacylglycerol hydrolase; monoglyceridyllipase; monoglyceridase; MLL; HU-K5; HUK5; MAGL; MGL; Lysophospholipase homolog; Lysophospholipase-like. Cat No: NATE-1638. | |
| Mouse factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig...factor VIIIa/IXa/Ca2+/phospholipid) which proteolytically activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. Purity: >95%. Factor IX. Mole weight: 55000. Storage: -20°C. Source: Mouse. Mouse factor IX; Factor IX. Pack: 50 ug. Cat No: CZY-032. | |
| Mouse Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fac...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Mouse glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...tly associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Mole weight: 88000. Stability: 12 months. Storage: -20°C. Source: Mouse. Mouse glu-Plasminogen; Plasminogen. Pack: 100 ug. Cat No: CZY-016. | |
| Mouse Prothrombin | Prothrombin is a vitamin K-dependent plasma protein which is synthesized in the liver. Prior to secretion into plasma, prothrombin undergoes post-translational modification by a vitamin K-dependent carboxylase which converts ten specific glutamic acid residues to γ-carboxyglutamic acid (gla). The ten gla residues are located within the first 40 amino acids of the mature protein and contribute to the ability of prothrombin to bind to negatively charged phospholipid membranes. Prothrombin contains two regions of internal homology which are referred to as "kringle" structures. These regions of conspicuous secondary structure are located between residues 40 and 270 of the mature p...-Ser321 (human) / Arg323-Ser324 (bovine) to a "pro" fragment (fragment 1.2) and thrombin, the latter of which is composed of two chains covalently linked by a disulfide bond. In the case of human prothrombin/thrombin, there is an additional thrombin feed-back cleavage at Arg284-Thr285 resulting in an additional 13 amino acids being removed from the mature thrombin A chain.Human prothrombin is prepared from fresh frozen human plasma as described by Bajaj and coworkers. Bovine prothrombin is prepared from fresh bovine plasma using a modification of the procedure described by Owen and coworkers. Purified prothrombin is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20 | |
| nardilysin | Enzyme of 133 kDa from rat brain and testis. A homologue of pitrilysin containing the His-Phe-Leu-Glu-His zinc-binding sequence, and a highly acidic stretch of 71 residues. Unusually for a metalloendopeptidase, inhibited by bestatin, amastatin and N-ethylmaleimide. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: N-arginine dibasic convertase; NRD-convertase. Enzyme Commission Number: EC 3.4.24.61. CAS No. 292850-69-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4344; nardilysin; EC 3.4.24.61; 292850-69-2; N-arginine dibasic convertase; NRD-convertase. Cat No: EXWM-4344. | |
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