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| Product | Description | |
|---|---|---|
| Vialinin A | Vialinin A. Group: Biochemicals. Grades: Purified. CAS No. 858134-23-3. Pack Sizes: 1mg. US Biological Life Sciences. |  Worldwide |
| Vialinin A | Vialinin A is an inhibitor of ubiquitin-specific peptidase 4 (USP4), USP5/isopeptidase T (IsoT) and UCH-L1 deubiquitinating enzyme (DUB) activity (IC50 = 1.5, 5.9 and 22.3 μM, respectively), displaying no significant inhibitory effects on UCH-L3, USP2, and USP8 activity. Vialinin A has been shown to reduce the release of TNF-α (IC50 = 0.09 nM) from RBL-2H3 mast cells. Synonyms: 1,1'-(4,4'',5',6'-Tetrahydroxy[1,1':4',1''-terphenyl]-2',3'-diyl) benzeneacetic acid ester; Ganbajunin C. Grades: ≥98% by HPLC. CAS No. 858134-23-3. Molecular formula: C34H26O8. Mole weight: 562.57. |  |
| Vialinin A | Vialinin A (Terrestrin A) is a p-terphenyl compound with antioxidant properties [1]. Vialinin A is a potent inhibitor of TNF-α, USP4, USP5, and sentrin/SUMO-specific protease 1 (SENP1). Vialinin A (Terrestrin A) can be used for autoimmune diseases and cancer research [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Terrestrin A. CAS No. 858134-23-3. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-103435. |  |
| Bijou Vial | Bijou Vial. Product ID: PM-028. Product Keywords: Packaging Materials; Glass Packaging; PM-028; Bijou Vial. |  |
| Borosilicate Glass Serum Vials | Borosilicate Glass Serum Vials. Product ID: PM-026. Product Keywords: Packaging Materials; Glass Packaging; PM-026; Borosilicate Glass Serum Vials. | |
| Compound VIALININ A | Compound VIALININ A. Uses: For analytical and research use. Group: Impurity standards. CAS No. 858134-23-3. Molecular Formula: C34H26O8. Mole Weight: 562.57. Catalog: APB858134233. |  |
| Dram Vials | Dram Vials. Product ID: PM-027. Product Keywords: Packaging Materials; Glass Packaging; PM-027; Dram Vials. | |
| Injection Vials | Injection Vials. Product ID: PM-029. Product Keywords: Packaging Materials; Glass Packaging; PM-029; Injection Vials. | |
| Moulded Universal Vial | Moulded Universal Vial. Product ID: PM-030. Product Keywords: Packaging Materials; Glass Packaging; PM-030; Moulded Universal Vial. | |
| Oligo dT (12,16,18) BioGenomics Kit, dT12. Vial-01 | Oligo dT (12,16,18) BioGenomics Kit, dT12Vial-01. Group: Molecular Biology. Alternative Names: [dT12: 5TTTTTTTTTTTT-3. US Biological Life Sciences. | Worldwide |
| Oligo dT (12,16,18) BioGenomics Kit, dT16. Vial-02 | Oligo dT (12,16,18) BioGenomics Kit, dT16Vial-02. Group: Molecular Biology. Alternative Names: dt16: 5TTTTTTTTTTTTTTTT-3. US Biological Life Sciences. | Worldwide |
| Oligo dT (12,16,18) BioGenomics Kit, dT18. Vial-03 | Oligo dT (12,16,18) BioGenomics Kit, dT18Vial-03. Group: Molecular Biology. Alternative Names: dT18: 5TTTTTTTTTTTTTTTTTT-3]. US Biological Life Sciences. | Worldwide |
| PET Diagnostic Vials | PET Diagnostic Vials. Product ID: PM-046. Product Keywords: Packaging Materials; Plastic Packaging; PM-046; PET Diagnostic Vials. | |
| PET Ready to Use Vials | PET Ready to Use Vials. Product ID: PM-050. Product Keywords: Packaging Materials; Plastic Packaging; PM-050; PET Ready to Use Vials. | |
| Polypropylene Ready to Fill Vials | Polypropylene Ready to Fill Vials. Product ID: PM-051. Product Keywords: Packaging Materials; Plastic Packaging; PM-051; Polypropylene Ready to Fill Vials. | |
| Snap Glass Top Vials | Snap Glass Top Vials. Product ID: PM-031. Product Keywords: Packaging Materials; Glass Packaging; PM-031; Snap Glass Top Vials. | |
| Tubular Diagnostic Screw Neck Vials | Tubular Diagnostic Screw Neck Vials. Product ID: PM-032. Product Keywords: Packaging Materials; Glass Packaging; PM-032; Tubular Diagnostic Screw Neck Vials. | |
| Type 1 Moulded Injection Vials | Type 1 Moulded Injection Vials. Product ID: PM-033. Product Keywords: Packaging Materials; Glass Packaging; PM-033; Type 1 Moulded Injection Vials. | |
| 2-O-Sulphatase from Flavobacterium heparinum | The 2-O-sulphatase acts on 2-O-sulphated ?4,5-unsaturated termini of disaccharides, tetrasaccharides, etc., produced by lyase action on a glycosaminoglycan. Group: Enzymes. Synonyms: 2-O-Sulphatase; Sulphatase. Enzyme Commission Number: EC 3.1.6.-. 2-O-Sulphatase. Mole weight: 41.8 kDa. Form: The enzyme is stabilised with 0.2% BSA, 0.22 um sterile-filtered and dispensed into sterile vials. To preserve high activity, the enzyme solution is stored frozen at -60°C and is supplied world-wide as a frozen solution. Source: Flavobacterium heparinum (ATCC 13125). 2-O-Sulphatase; Sulphatase. Cat No: NATE-1943. |  |
| ?-4,5-Glycuronidase from Flavobacterium heparinum | The ?-4,5-Glycuronidase acts on the non-sulphated, unsaturated termini of disaccharides, tetrasaccharides, etc., produced either directly by lyase action on a glycosaminoglycan or by the action of the 2-O-sulphatase on an unsaturated disaccharide, tetrasaccharide, etc. Group: Enzymes. Synonyms: ?-4,5-Glycuronidase; Glycuronidase. Enzyme Commission Number: EC 3.2.1-. β-Glucosidase. Storage: Store frozen at -20 or below upon receipt. Avoid repeated freezethawing. Form: The enzyme is stabilised with 0.2% BSA, 0.22 um sterile-filtered and dispensed into sterile vials. To preserve high activity, the enzyme solution is stored frozen at -60°C and is supplied world-wide as a frozen solution. Source: Flavobacterium heparinum (ATCC 13125). ?-4,5-Glycuronidase; Glycuronidase. Cat No: NATE-1942. | |
| 5'-Nucleotidase from Human, Recombinant | 5'-nucleotidase is an extracellular enzyme that converts nucleoside-5'-monophosphates to nucleosides with a substrate preference of AMP. Native 5'-nucleotidase is a GPI-anchored protein whose exporession is upregulated by hypoxia. 5'-nucleotidase has many functions in vivo including the generation of extracellular adenosine. 5'-Nucleotidase has various clinical significances. It is a key molecule in the regulation of cancer cells proliferation, migration and invasion in vitro tumor angiogenesis, and tumor immune escape in vivo. Due to this important role, the enzyme is a potential target for cancer research.1 It is also involved in salvage of extracellular nucleotides and...Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. Purity: >90% (SDS-PAGE). AMPase. Mole weight: ~61 kDa by SDS-PAGE (reducing). Activity: >15 U/mg. Storage: Store at -70°C. Form: Supplied as a solution containing Tris, NaCl, CaCl2, and 20% glycerol. Source: CHO cells. Species: Human. uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5; CD73; NT5E; ecto-5'-nucleotidase. Pack: vial of 6-12 μg. Cat No: NATE-0795. | |
| Active Focal Adhesion Kinase from Human, Recombinant | FAK is a cytoplasmic protein tyrosine kinase which is found concentrated in the focal adhesions that form between cells growing in the presence of extracellular matrix constituents. The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Activation of this gene may be an important early step in cell growth and intracellular signal transduction pathways triggered in response to certain neural peptides or to cell interactions with the extracellular matrix. At least four transcript variants encoding four different isoforms have been found for this gene, but the full-le...Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Enzyme Commission Number: EC 2.7.10.2. Purity: Greater than 70% as determined by SDS-PAGE. FAK. Mole weight: 146.7 kDa. Activity: 72 nmole of phosphate transferred to poly [Glu,Tyr] 4:1 substrate/minute/mg of total protein at 30°C. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C to -80°C for longer periods of time. Avoid multiple freeze-thaw cycles. Source: Baculovirus, SF9 insect cells. Species: Human. Focal adhesion kinase 1; EC 2.7.10.2; FADK 1; pp125FAK; Protein-tyrosine kinase 2; FAK; FADK; FAK1; PTK2; FRNK; PPP1R71; p125FAK. Cat No: NATE-0800. | |
| Aldehyde Dehydrogenase 2 from Human, Recombinant | ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial... & having a molecular mass of 54.5 kda. the aldh2 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Purity: Greater than 90.0% as determined by SDS-PAGE. ALDH2. Mole weight: 54.5 kDa. Activity: > 0.14 units/ml. Stability: Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Cat No: NATE-0804. | |
| Allene Oxide Synthase from Parthenium argentatum, Recombinant | Potent anti-oxidant enzyme to remove lipid hydroperoxides in biological samples. Allene oxide synthase converts lipoxygenase derived fatty acid hydroperoxides to unstable allene epoxides. In plants, allene oxide is a precursor of jasmonic acid, which is important for growth regulation. Applications: Allene oxide synthase is a potent anti-oxidant enzyme used to remove lipid hydroperoxides in various biological samples. it may also be used to study stress induced gene expression in plants. Group: Enzymes. Synonyms: hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydr. Enzyme Commission Number: EC 4.2.1.92. AOS. Activity: 25,000-40,000 units/mg protein. Storage: Store at -20°C. Form: Supplied as a solution in phosphate buffered sale pH 7.2. Source: E. coli. Species: Parthenium argentatum. hydroperoxide isomerase; linoleate hydroperoxide isomerase; linoleic acid hydroperoxide isomerase; HPI; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase; (9Z,11E,14Z)-(13S)-hydroperoxyoctadeca-9,11,14-trienoate 12,13-hydro-lyase [(9Z)-(13S)-12,13-epoxyoctadeca-9,11-dienoate-forming]; allene oxide synthase; AOS; EC 4.2.1.92; hydroperoxide dehydratase. Pack: vial of ~300 μg. Cat No: NATE-0808. | |
| 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 | |
| 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. | |
| ATTO 665 NHS ester | ATTO 665 is a new fluorescent label closely related to ATTO 647N. It shows extraordinary high fluorescence quantum yield, excellent thermal and photo-stability, outstanding ozone resistance, and very little triplet formation. ATTO 665 is a cationic (charge +1). The dye is moderately hydrophilic. The NHS-ester of the dye reacts easily with amino-groups of proteins and other bio-molecules. Since the amino group must be non protonated to be reactive, the pH of the reaction is recommended to be about 8.3. Prepare labeling solution of NHS-ester immediately before use by dissolving the vial content in anhydrous and amine-free DMF or DMSO.find more information here. | |
| β-(1?3,4,6)-Galactosidase from Streptococcus pneumoniae and Xanthomonas sp., Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Group: Enzymes. Synonyms: β-(1?3,4,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 70 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Streptococcus pneumoniae and Xanthomonas sp. β-(1?3,4,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: vial of 0.24 unit. Cat No: NATE-0299. | |
| β-(1?3,6)-Galactosidase from Xanthomonas manihotis, Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Recombinant, expressed in e. coli, buffered aqueous solution. Group: Enzymes. Synonyms: β-(1?3,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 120 units/mg protein. Stability: 2-8°C. Form: buffered aqueous solution. Source: E. coli. Species: Xanthomonas manihotis. β-(1?3,6)-Galactosidase; β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: vial of 1.9 units. Cat No: NATE-0301. | |
| β (1?4)-Galactosidase from Streptococcus pneumoniae, Recombinant | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Recombinant, expressed in e. coli, buffered aqueous solution. Group: Enzymes. Synonyms: β (1?4)-Galactosidase; 9031-11-2; β-Galactosidase; beta-gal; β-gal; GLB; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 6 units/mg protein. Stability: 2-8°C. Form: buffered aqueous solution. Source: E. coli. Species: Streptococcus pneumoniae. β (1?4)-Galactosidase; 9031-11-2; β-Galactosidase; beta-gal; β-gal; GLB; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Pack: vial of 0.06 unit. Cat No: NATE-0300. | |
| β-Lactamase Blend, Recombinant | β--lactamase inactivates β-lactam antibiotics by breaking open the β-lactam ring. Group: Enzymes. Synonyms: β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Enzyme Commission Number: EC 3.5.2.6. CAS No. 9073-60-3. β-Lactamase. Activity: 600-1500 IU beta-lactamase I per vial; 60-100 IU beta-lactamase II per vial. Storage: 2-8°C. Form: Lyophilized powder containing sodium chloride, potassium phosphate and sorbitol. Source: E. coli. β-lactamase; penicillinase; cephalosporinase; neutrapen; penicillin β-lactamase; exopenicillinase; ampicillinase; penicillin amido-β-lactamhydrolase; penicillinase I, II; β-lactamase I-III; β-lactamase A, B, C; β-lactamase AME I; cephalosporin-β-lactamase; EC 3.5.2.6; 9073-60-3. Cat No: NATE-0776. | |
| β-N-Acetylglucosaminidase from Streptococcus pneumoniae, Recombinant | Hexosaminidase, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Appli...Commission Number: 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: > 80 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Streptococcus pneumoniae. EC 3.2.1.52; 9012-33-3; hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase. Pack: vial of > 1.0 unit. Cat No: NATE-0782. | |
| Cathepsin S from Human, recombinant | Cathepsin S (CTSS) is a lysosomal cysteine protease of the papain family and may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. The deduced amino acid sequence contains only one potential N-glycosylation site located in the propeptide. Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung...l compartment, and is implicated in the pathogenesis of Alzheimers disease and Down Syndrome. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CAS No. 71965-46-3. Purity: > 90% by SDS-PAGE. CTSS. Mole weight: 23.9 kDa (115-331 aa). Activity: >2000 mU/mg. Storage: Stable for at least 1 year as supplied. Briefly spin down the vial and reconstitute in 50 mM sodium acetate, 100 mM NaCl (pH 5.5) to 0.1-1 mg/ml and store at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized from proprietary buffer. Source: E. coli. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-1702. | |
| Chondroitinase B from Flavobacterium heparinum, Recombinant | In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAc-4S). This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The enzyme cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroit...preparation of di-and oligo-saccharides of dermatan sulfate. Group: Enzymes. Synonyms: Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Enzyme Commission Number: EC 4.2.2.19. CAS No. 52227-83-5. Purity: > 90 % by reversed phase HPLC analysis. ChonB. Mole weight: 54,779 Da. Activity: > 550 IU/mg (substrate: dermatan sulfate). Stability: Expiration is 30 months from manufacturing date, frozen at -70°C in aqueous buffers containing Sodium Chloride, Sodium Phosphate and Sucrose 5%. Source: Flavobacterium heparinum. Species: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Pack: vial of 5 ug. Cat No: NATE-0130. | |
| Collagenase/Neutral Protease Blend (GMP Grade) | NATE-1917 is an avian and mammalian tissue-free Collagenase and neutral protease enzyme blend produced under GMP quality conditions. Applications: Nate-1917 is specifically designed for stem cell isolation from human and other adipose tissue with following advantages:o a single, sterile, ready-to-use vial containing both collagenase and neutral protease can digest up to 280g of adipose tissue with best-in-class gmp quality and shelf life of up to 72 months.o currently included in ide applications approved by the u.s. fda for alopecia, chronic heart failure, hamstring injuries, osteoarthritis of the knee, and hand manifestations of scleroderma.o research protocols are a...sociation of nucleated cells from adipose tissue.o produced using avian and mammalian tissue-free raw materials, aseptic processes and sterile filtration under gmp guidelines to assure the lowest levels of impurities and stringent quality standards. Group: Enzymes. Synonyms: Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Collagenase. Stability: 48 months at -15 to -25° C. Appearance: White lyophilizate. Source: Clostridium histolyticum/Bacillus polymyxa. Collagenase/Neutral Protease Blend; GMP, Collagenase/Neutral Protease Blend; Collagenase; Neutral Protease; GMP. Pack: 1 vial, 35 mg. Cat No: NATE-1917. | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| Fumarate Hydratase from Human, Recombinant | Fumarase catalyzes the reversible hydration of fumarate to malate. In its mitochondrial form, fumarate is involved in the Krebs Cycle, while the cytosolic form is involved in amino acid metabolism. Group: Enzymes. Synonyms: EC 4. 2. 1. 2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6; MCL; LRCC; HLRCC; MCUL1; FH. Enzyme Commission Number: EC 4. 2. 1. 2. Purity: >95% by SDS-PAGE analysis. Mole weight: 50.2 kDa. Activity: >25 unit/mg. Storage: 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. EC 4. 2. 1. 2; fumarase; L-malate hydro-lyase; (S)-malate hydro-lyase; 9032-88-6; MCL; LRCC; HLRCC; MCUL1; FH; Fumarate hydratase. Cat No: NATE-1777. | |
| Glutathione S-Transferase Alpha 4 (GSTa4) Recombinant, Mouse, Positive Control Loading Buffer | Glutathione S-Transferase Alpha 4 (GSTa4) Recombinant, Mouse, Positive Control Loading Buffer. Group: Molecular Biology. Grades: Highly Purified. Pack Sizes: 1x1 vial. US Biological Life Sciences. | Worldwide |
| Glutathione S-Transferase from E.coli, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to iden...ferase. Mole weight: 26kDa. Activity: >20 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 clear solution in Phosphate Buffered Saline pH 7.4. Source: E.coli. Species: E.coli. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1945. | |
| Granzyme A from Human, Recombinant (carrier-free) | Granzyme A is a serine protease belonging to the granzyme family and is expressed exclusively by cytotoxic T cells (CTL) and NK cells. Most circulating CD56+CD8- NK cells, and approximately half of circulating CD8+ T cells, coexpress both granzymes A and B. Group: Enzymes. Synonyms: Hanukah factor serine protease (HFSP); Cytolytic T cell-and natural killer cell-specific trypsin-like serine protease; Cytotoxic T-lymphocyte-associated serine esterase 3; CTLA3; Granzyme A; Granzyme. Enzyme Commission Number: EC 3.4.21.78. CAS No. 143180-73-8. Purity: >90%, as determined by Coomassie stained SDS-PAGE. Granzyme A. Mole weight: 55 kD in non-reducing conditions by SDS-PAGE. Activity: >5,000 pmol/min/ug. Storage: Unopened vial can be stored at -70°C for six months. For maximum results, quick spin vial prior to opening. Avoid repeated freeze/thaw cycles. Form: 0.22 um filtered protein solution is in 20 mM Tris, 150 mM NaCl, pH 7.5. Source: 293E cell line. Species: Human. Hanukah factor serine protease (HFSP); Cytolytic T cell-and natural killer cell-specific trypsin-like serine protease; Cytotoxic T-lymphocyte-associated serine esterase 3; CTLA3; Granzyme A; Granzyme. Cat No: NATE-1934. | |
| G/U Mismatch-Specific DNA Glycosylase from E.coli, Recombinant | G/U mismatch-specific DNA glycosylase (mug) is a part of the TDG/mug DNA glycosylase family. Mug is necessary for DNA damage lesion repair in stationary-phase cells. Mug protein removes three N4-ethenocytosine and takes away s the uracil base from mismatches in the order of U:G>U:A. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP position. Mug is also able to hydrolyzing the carbon-nitrogen bond among the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine plays a role in substrate recognition. Group: Enzymes. Synonyms: Xanthine DNA glycosylase; dug; ECK3058; JW3040; ygjF; G/U mismatch-specific DNA glycosylase; Double-strand-specific uracil glycosylase; Mismatch-specific uracil DNA-glycosylase; mug. Enzyme Commission Number: EC 3.2.2.28. Purity: Greater than 90% as determined by SDS-PAGE. MUG. Mole weight: 21.1 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. Form: Sterile Filtered colorless solution. Source: E.coli. Species: E.coli. Cat No: NATE-1911. | |
| Hexokinase-1 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk1 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag a...ferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 104.6 kDa. Activity: 7-8 units/ml. 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). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-1; EC 2.7.1.1; Hexokinase type I; HK I; Brain form hexokinase; HK1-ta; HK1-tb; HXK1; HK1. Cat No: NATE-0844. | |
| Hexokinase-2 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk2 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag a...rase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 90.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 104.1 kDa. Activity: 3-4 units/ml. 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). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-2; EC 2.7.1.1; HK2; Hexokinase type II; HK II; Muscle form hexokinase; HXK2; DKFZp686M1669. Cat No: NATE-0845. | |
| Hexokinase-3 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Hk-3 human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to his tag ...phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Hexokinase. Mole weight: 101.1 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). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Hexokinase-3; EC 2.7.1.1; Hexokinase type III; HK III; HXK3; HK3. Cat No: NATE-0846. | |
| Hexokinase-4 from Human, Recombinant | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Glucokinase human recombinant produced in e. coli is a single, non-glycosylated, polypeptide chain fused to h...se; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: Greater than 95.0% as determined by SDS-PAGE. Hexokinase. Mole weight: 54.3 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). Please avoid freeze-thaw cycles. Appearance: Sterile filtered colorless solution. Source: E. coli. Species: Human. Glucokinase; EC 2.7.1.2; Hexokinase-4; Hexokinase type IV; HK IV; HK4; Hexokinase-D; GCK; GK; GLK; HHF3; HKIV; HXKP; MODY2. Cat No: NATE-0847. | |
| HIV Protease Mutant, Recombinant | HIV-1 protease is a retroviral aspartyl protease (retropepsin) that is essential for the life-cycle of HIV, the retrovirus that causes AIDS. HIV protease cleaves newly synthesized polyproteins at the appropriate places to create the mature protein components of an infectious HIV virion. Without effective HIV protease, HIV virions remain uninfectious. Thus, mutation of HIV protease's active site or inhibition of its activity disrupts HIVs ability to replicate and infect additional cells, making HIV protease inhibition the subject of considerable pharmaceutical research. Group: Enzymes. Synonyms: human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease; HIV-1 retropepsin; HIV Protease Mutant; EC 3.4.23.16. Enzyme Commission Number: EC 3.4.23.16. CAS No. 144114-21-6. HIV Protease. Mole weight: mol wt ~10.8 kDa. Storage: -70°C. Form: Supplied as a solution in 0.5M Sodium Acetate, pH 4.7with 50mM Tris-HCL, 1M NaCL, 1mM EDTA, 5mM DTT and 15% glycerol. Source: E. coli. human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease; HIV-1 retropepsin; HIV Protease Mutant; EC 3.4.23.16. Pack: 100 unit vial containing > 100ug protein. Cat No: NATE-0344. | |
| Inosine Monophosphate Dehydrogenase Type II from Human, Recombinant | Type II is the predominant IMPDH isoform and is specifically linked to a wide range of cancers and lymphocyte proliferation. Group: Enzymes. Synonyms: inosine-5'-phosphate dehydrogenase; inosinic acid dehydrogenase; inosinate dehydrogenase; inosine 5'-monophosphate dehydrogenase; inosine monophosphate dehydrogenase; IMP oxidoreductase; inosine monophosphate oxidoreductase; IMP dehydrogenase; IMP:NAD+ oxidoreductase; EC 1.1.1.205; IMPDH II; IMPDH2; IMPD 2. Enzyme Commission Number: EC 1.1.1.205. CAS No. 231-791-2. IMPDH2. Storage: -70°C. Form: Solution in 20 mM Tris-HCl, pH 8.0, containing 0.5 mM EDTA and 1 mM DTT. Source: E. coli. Species: Human. inosine-5'-phosphate dehydrogenase; inosinic acid dehydrogenase; inosinate dehydrogenase; inosine 5'-monophosphate dehydrogenase; inosine monophosphate dehydrogenase; IMP oxidoreductase; inosine monophosphate oxidoreductase; IMP dehydrogenase; IMP:NAD+ oxidoreductase; EC 1.1.1.205; IMPDH II; IMPDH2; IMPD 2. Pack: vial of > 0.002 unit. Cat No: NATE-0352. | |
| METHYL SORBATE | METHYL SORBATE. Synonyms: METHYL T2 T4 HEXADIENOATE;2,4-HEXADIENOIC ACID METHYL ESTER;METHYL 2,4-HEXADIENOATE;FEMA 3714;SORBIC ACID METHYL ESTER;methyl hexa-2,4-dienoate;2,4-Hexadienoic acid methyl;Hexa-2,4-dienoic acid methyl ester. CAS No. 1515-80-6. Product ID: CDF4-0117. Molecular formula: C7H10O2. Category: Food Preservatives. Product Keywords: Food Ingredients; Food Preservatives; METHYL SORBATE; CDF4-0117; 1515-80-6; C7H10O2; 216-160-1; 1515-80-6. Purity: 0.98. Color: Colourless. EC Number: 216-160-1. Physical State: Oil. Solubility: Chloroform (Sparingly), Ethyl Acetate, Methanol (Slightly). Storage: Amber Vial, Refrigerator. Boiling Point: 180 °C(lit.). Melting Point: 8°C. | |
| Mitogen activated protein kinase from rat, Recombinant | Mitogen-activated protein kinases (MAPK) are protein kinases that are specific to the amino acids serine, threonine, and tyrosine. MAPKs belong to the CMGC (CDK/MAPK/GSK3/CLK) kinase group. MAPKs are involved in directing cellular responses to a diverse array of stimuli, such as mitogens, osmotic stress, heat shock and proinflammatory cytokines. They regulate cell functions including proliferation, gene expression, differentiation, mitosis, cell survival, and apoptosis. > 95% (sds-page), buffered aqueous glycerol solution, recombinant, expressed in e. coli (n-terminal histidine tagged). Group: Enzymes. Synonyms: ERK2; Extracellular-signal regulated kinase; MAP Kinase Activated from rat; MAPK; Mitogen activated protein kinase. Purity: > 95% (SDS-PAGE). MAP kinase. Mole weight: mol wt 42 kDa. Activity: > 500 U/mg. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: E. coli. Species: Rat. ERK2; Extracellular-signal regulated kinase; MAP Kinase Activated from rat; MAPK; Mitogen activated protein kinase. Pack: vial of 100 ng. Cat No: NATE-0443. | |
| Native α-1,2-Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1,2-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 0.4 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. α-1,2-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Pack: vial of 0.004 unit. Cat No: NATE-0259. | |
| Native Bacillus licheniformis NADH Oxidase | NADH Oxidase from Bacillus licheniformis was shown to display hydrogen peroxide-forming activity. Nadh oxidase is a surface enzyme with increased oxidative activity in polymorphonuclear leukocytes during phagocytosis. Applications: Nadh oxidase from bacillus licheniformis has been used in a study to assess nitrogen assimilation by bacillus licheniformis growing in chemostat cultures. it has also been used in a study to investigate the role of glutamate dehydrogenase in ammonia assimilation in bacillus macerans. Group: Enzymes. Synonyms: NADH Oxidase; 9032-21-7. CAS No. 9032-21-7. NADH Oxidase. Activity: > 35 units/mg protein. Form: lyophilized powder. Source: Bacillus licheniformis. NADH Oxidase; 9032-21-7. Pack: vial of > 15 units. Cat No: NATE-0473. | |
| Native Bovine Protein Phosphatase 2A1 | Protein Phosphatase 2A1 is a trimer consisting of the A, B, and C subunits of the PP2A family. It has a total molecular weight of 192 kDa. Protein Phosphatase 2A is a cytoplasmic protein, which colocalizes with mictotubule proteins and is involved in the dephosphorylation of the tau protein and oncoprotein 18. Protein Phosphatase 2A1 binds to polymerized microtubule proteins and may be targeted by tubulin in modulating phosphatase activity. Applications: Protein phosphatase 2a1 is a divalent cation-dependent protein serine/threonine phosphatase implicated as a growth suppressor and is associated with dis-regulation in cancer. the enzyme is involved in regulating numerous cellular processes and is used to study cell cycle, growth, and differentiation. the protein phosphatase 2a1 has been used to treat human fibroblast cells prior to western blot analysis. Group: Enzymes. Synonyms: Protein Phosphatase 2A1; PP2A1; PPA2A1. Purity: >90% (SDS-PAGE). Protein Phosphatase. Activity: > 1500 units/mg protein. Stability: -70°C. Form: Solution in 50 mM Tris-HCl, pH 7.0, containing 14 mM 2-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol. Source: Bovine. Protein Phosphatase 2A1; PP2A1; PPA2A1. Pack: vial of 1 μg. Cat No: NATE-0616. | |
| Native Bovine Protein Phosphatase 2C | Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619. | |
| Native Crotalus adamanteus venom Phosphodiesterase I | Venom exonuclease (Phosphodiesterase I) successively hydrolyzes 5'-mononucleotides from 3'-OH-terminated ribo- and deoxyribo-oligonucleotides. The enzyme has an optimal pH range of 9.8-10.4 and a molecular weight of 115 kDa. Phosphodiesterase is inhibited by reducing agents such as glutathione, cysteine and ascorbic acids. It is completely inhibited by 5mM EDTA while ATP, ADP and AMP are partial inhibitors. The enzyme has an absolute requirement for Mg2+. Group: Enzymes. Synonyms: Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodies. Enzyme Commission Number: EC 3.1.4.1. CAS No. 9025-82-5. PDE. Activity: > 20 units per mg dry weight. Storage: -20°C. Form: Lyophilized in vials. Source: Crotalus adamanteus venom. Phosphodiesterase I; EC 3.1.4.1; 5'-exonuclease; 5'-phosphodiesterase; 5'-nucleotide phosphodiesterase; oligonucleate 5'-nucleotidohydrolase; 5' nucleotide phosphodiesterase/alkaline phosphodiesterase I; 5'-NPDase; 5'-PDase; 5'-PDE; 5'NPDE; alkaline phosphodiesterase; nucleotide pyrophosphatase/phosphodiesterase I; orthophosphoric diester phosphohydrolase; PDE I; phosphodiesterase; exonuclease I. Cat No: NATE-0512. | |
| Native Crotalus adamanteus venom Pyrophosphatase, Nucleotide | In enzymology, a nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction:a dinucleotide + H2O<-> 2 mononucleotides. Thus, the two substrates of this enzyme are dinucleotide and H2O, whereas its product is mononucleotide. This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. This enzyme participates in 5 metabolic pathways:purine metabolism, starch and sucrose metabolism, riboflavin metabolism, nicotinate and nicotinamide metabolism, and pantothenate and coa biosynthesis. Group: Enzymes. Synonyms: nucleotide diphosphatase; EC 3.6.1.9; nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase; 9032-64-8. Enzyme Commission Number: EC 3.6.1.9. CAS No. 9032-64-8. Nucleotide Pyrophosphatase. Activity: 4-8 units/mg protein, vial of ~25 units. Storage: -20°C. Form: Lyophilized powder containing approx. 35% Tris buffer salts. Source: Crotalus adamanteus venom. nucleotide diphosphatase; EC 3.6.1.9; nucleotide pyrophosphatase; nucleotide-sugar pyrophosphatase; 9032-64-8. Pack: vial of ~25 units. Cat No: NATE-0493. | |
| Native Galactose-adapted yeast Uridine-5'-diphosphogalactose 4-epimerase | The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Group: Enzymes. Synonyms: UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-gal. Enzyme Commission Number: EC 5.1.3.2. CAS No. 9032-89-7. UDP-Glc 4-epimerase. Activity: 10-20 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 40% buffer salts. Source: Galactose-adapted yeast. UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase; EC 5.1.3.2; UDP-glucose 4-epimerase; GALE. Pack: vial. Cat No: NATE-0275. | |
| Native Human Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Applications: Trypsin has been used in a study to assess the similarities between the hepatitis e virus and human astrovirus. trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; trypta. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Trypsin. Activity: vial of > 1 ,000 BAEE units. Storage: 2-8°C. Form: salt-free, lyophilized powder. Source: Human pancreas. Species: Human. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin. Cat No: NATE-0722. | |
| Native Mouse Endoproteinase Arg-C | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| Native Penicillium citrinum Nuclease P1 | Nuclease P1 from Penicillium citrinum is a zinc-dependent endonuclease that exhibits increased activity in the presence of low concentrations of urea. Applications: Nuclease p1 from penicillium citrinum has been used in a study to assess crystal structures using ammonium sulphate or polyethylene glycol 4000 as a precipitating agent. it has also been used in a study to investigate a method for the direct sequence analysis 20-25 nucleotides from the terinini of 5? or 3? end group labeled rna. nuclease p1 is used to improve the sensitivity of a 32p-labeling method for the detection of dna adducts. the enzyme has an optimal temperature of approximately 70 oc, but for a long incubation, a temperature below 60 oc is more suitable. it is stable in the ph range of 5-8. Group: Enzymes. Synonyms: Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Enzyme Commission Number: EC 3.1.30.1. CAS No. 54576-84-0. Nuclease. Mole weight: 42-50 kDa. Activity: > 200 units/mg protein (E1%/280, 3?-5?-Phosphodiesterase). Storage: 2-8°C. Form: lyophilized powder. Source: Penicillium citrinum. Endonuclease P1; EC 3.1.30.1; 54576-84-0; Nuclease P1; P1 nuclease. Pack: vial of > 250 units (using RNA substrate). Cat No: NATE-0491. | |
| Native Penicillium janthinellum Carboxypeptidase P | Membrane Pro-Xaa carboxypeptidase (EC 3.4.17.16, carboxypeptidase P, microsomal carboxypeptidase) is an enzyme. This enzyme catalyses the following chemical reaction:Release of a C-terminal residue other than proline, by preferential cleavage of a prolyl bond. This is one of the renal brush border exopeptidases. Applications: Membrane pro-xaa carboxypeptidase (ec 3.4.17.16, carboxypeptidase p, microsomal carboxypeptidase) is an enzyme.[1][2][3] this enzyme catalyses the following chemical reaction release of a c-terminal residue other than proline, by preferential cleavage of a prolyl bond this is one of the renal brush border exopeptidases. Group: Enzymes. Synonyms: Aminoacylproline Carboxypeptidase; CPP; Penicillocarboxypeptidase S-1; Proline Carboxypeptidase; EC 3.4.17.16; Membrane Pro-Xaa carboxypeptidase; carboxypeptidase P; microsomal carboxypeptidase. Enzyme Commission Number: EC 3.4.17.16. CAS No. 9075-64-3. CPP. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate. Source: Penicillium janthinellum. Aminoacylproline Carboxypeptidase; CPP; Penicillocarboxypeptidase S-1; Proline Carboxypeptidase; EC 3.4.17.16; Membrane Pro-Xaa carboxypeptidase; carboxypeptidase P; microsomal carboxypeptidase. Pack: vial of > 100 units. Cat No: NATE-0157. | |
| Native Pseudomonas fragi mutant strain Endoproteinase Asp-N | Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Cleavage of Xaa-Asp, Xaa-Glu and Xaa-cysteic acid bonds. This metalloenzyme is isolated from Pseudomonas fragi. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 9001-92-7. Endoproteinase Asp-N. Storage: 2-8°C. Form: lyophilized powder. Source: Pseudomonas fragi mutant strain. endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Pack: vial of 2 μg. Cat No: NATE-0222. | |
| Native Pseudomonas sp. Keratanase | Keratan-sulfate endo-1,4-beta-galactosidase (EC 3.2.1.103, endo-beta-galactosidase, keratan sulfate endogalactosidase, keratanase, keratan-sulfate 1,4-beta-D-galactanohydrolase) is an enzyme with system name keratan-sulfate 4-beta-D-galactanohydrolase. This enzyme catalyses the following chemical reaction:Endohydrolysis of (1->4)-beta-D-galactosidic linkages in keratan sulfate. Hydrolyses the 1,4-beta-D-galactosyl linkages adjacent to 1,3-N-acetyl-alpha-D-glucosaminyl residues. Group: Enzymes. Synonyms: Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Enzyme Commission Number: EC 3.2.1.103. CAS No. 55072-01-0. Endo-β-galactosidase. Storage: -20°C. Form: lyophilized powder. Source: Pseudomonas sp. Endo-β-galactosidase; endo-β-galactosidase; keratan sulfate endogalactosidase; keratanase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Pack: vial of >10 units. Cat No: NATE-0364. | |
| Native Rat Protein Kinase C Catalytic Subunit | Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second family are phospholipid-dependent but Ca2+-independent, and include PKCδ, ε, η, and &theta. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Does not require ca2+ or phosphatidylserine for its activity. Group: Enzymes. Synonyms: PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Purity: > 90% (SDS-PAGE). PKC. Activity: > 800 units/mg protein. Stability: -70°C. Source: rat brain. Species: Rat. PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Pack: vial of 200 ng. Cat No: NATE-0578. | |
| Native Xanthomonas sp. α-1? (2,3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1? (2,3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 0.5 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: Xanthomonas sp. α-1? (2,3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Pack: vial of 0.004 unit. Cat No: NATE-0262. | |
| Native Xanthomonas sp. α-1? (3,4) Fucosidase solution | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1? (3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: Xanthomonas sp. α-1? (3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; EC 3.2.1.51; 9037-65-4. Pack: vial of 0.02 unit. Cat No: NATE-0263. | |
| Neuronal Specific Enolase (His Tag) from Human, Recombinant | NSE is the γ isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival. Neuron specific enolase human recombinant is expressed in e. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag. the nse is purified by proprietary chromatographic ...y: Greater than 95% as determined by SDS-PAGE. Single band on Western Blot. Enolase. Stability: Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. EC 4.2.1.11; Neuron Specific Enolase; NSE; enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydratase; 2-phosphoglycerate dehydratase; 2-phosphoglyceric dehydratase; 2-phosphoglycerate enolase; γ-enolase; 2-phospho-D-glycerate hydro-lyase; phosphopyruvate hydratase. Cat No: NATE-0903. | |
| Nitrate Reductase from Arabidopsis thaliana, Recombinant | Nitrate reductase (NADH) is an enzyme with system name nitrite:NAD+ oxidoreductase. This enzyme catalises the following chemical reaction:nitrite + NAD+ + H2O<-> nitrate + NADH + H+. Nitrate reductase us an iron-sulfur molybdenum flavoprotein. Applications: Catalyzes the nadh-dependent reduction of nitrate to nitrite. nitrate reductase from arabidopsis thaliana has been used in a study to assess the amino acid sequence of chicken hepatic sulfite oxidase. Group: Enzymes. Synonyms: Nitrate reductases; assimilatory nitrate reductase; NADH-nitrate reductase; NADH-dependent nitrate reductase; assimilatory NADH:nitrate reductase; nitrate reductase (NADH2); NADH2:nitrate oxidoreductase; nitrate reductase (NADH); EC 1.7.1.1. Enzyme Commission Number: EC 1.7.1.1. CAS No. 9013-03-0. Nitrate reductase. Activity: vial of > 0.5 unit. Storage: -20°C. Form: Supplied as a lyophilized powder containing 50 mM MOPS, pH 7.0, 1 mM EDTA and a proprietary sugar. Source: Pichia pastoris. Species: Arabidopsis thaliana. Nitrate reductases; assimilatory nitrate reductase; NADH-nitrate reductase; NADH-dependent nitrate reductase; assimilatory NADH:nitrate reductase; nitrate reductase (NADH2); NADH2:nitrate oxidoreductase; nitrate reductase (NADH); EC 1.7.1.1. Pack: vial of > 0.5 unit. Cat No: NATE-0486. | |
| Peptidase D from Human, Recombinant | PEPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 56.9kDa.PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques. Peptidase d, also known as pepd, is a part of the peptidase family. pepd is involved in collagen metabolism due to the high level of iminoacids in collagen. pepd recycles proline, and sets the pace for the production of collagen. pepd is also parts dipeptides with a prolyl or hydroxyprolyl residue in the c-terminal position. Group: Enzymes. Synonyms: Xaa-Pro dipeptidase; X-Pro dipeptidase; Imidodipeptidase; Peptidase D; Proline dipept. Enzyme Commission Number: EC 3.4.13.9. CAS No. 9025-32-5. Purity: Greater than 90% as determined by SDS-PAGE. Prolidase. Mole weight: 56.9kDa. Storage: 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. Xaa-Pro dipeptidase; X-Pro dipeptidase; Imidodipeptidase; Peptidase D; Proline dipeptidase; Prolidase; PRD; PEPD; Xaa-Pro dipeptidase isoform 1; PROLIDASE; Peptidase D; PEPD. Cat No: NATE-1782. | |
| Peptidyl-Prolyl Cis/Trans Isomerase from Human, Recombinant | Human Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor...ase Pin1; DOD; UBL5; PIN1; PPIase. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. Peptidylprolyl Isomerase. Mole weight: 18.2 kDa. Activity: > 162 nmoles/min/ug. 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 colorless solution. Source: E. coli. Species: Human. Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; EC 5.2.1.8; Rotamase Pin1; PPIase Pin1; DOD; UBL5; PIN1; PPIase. Cat No: NATE-0910. | |
| Phosphoserine Phosphatase from Human, Recombinant | Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated-helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis. Phosphoserine phosphatase human recombinant produced in e. coli is a single, non-glycosylated polypeptid...3-phosphoserine phosphatase; PSPH. Enzyme Commission Number: EC 3.1.3.3. CAS No. 9025-73-4. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. PSP. Mole weight: 25 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 colorless solution. Source: E. coli. Species: Human. Phosphoserine phosphatase; EC 3.1.3.3; PSP; O-phosphoserine phosphohydrolase; PSPase; L-3-phosphoserine phosphatase; PSPH. Cat No: NATE-0911. | |
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