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| Product | Description | |
|---|---|---|
| HUMAN DES(1-6)IGF-II | HUMAN DES(1-6)IGF-II. Uses: Designed for use in research and industrial production. Additional or Alternative Names: DES (1-6) IGF II;HUMAN DES(1-6)IGF-II;des (1-6) insulin-like growth factor ii;IGF-II (Δ 1-6);Insulin-like Growth Factor-II (Δ 1-6) human. Product Category: Heterocyclic Organic Compound. CAS No. 141909-47-9. Purity: 0.96. Product ID: ACM141909479. Alfa Chemistry ISO 9001:2015 Certified. |  |
| Human drosomycin-like defensin | Human drosomycin-like defensin is an antibacterial peptide isolated from Homo sapiens. It has activity against fungi. Synonyms: Cys-Leu-Ala-Gly-Arg-Leu-Asp-Lys-Gln-Cys-Thr-Cys-Arg-Arg-Ser-Gln-Pro-Ser-Arg-Arg-Ser-Gly-His-Glu-Val-Gly-Arg-Pro-Ser-Pro-His-Cys-Gly-Pro-Ser-Arg-Gln-Cys-Gly-Cys-His-Met-Asp. |  |
| Human Endogenous Metabolite Library | A unique collection of 1400 endogenous metabolism-related compounds for research in endogenous metabolism-related diseases and drug screening; - Effective tool for research in endogenous metabolism-related diseases, exploring the tumorigenesis, and drug discovery; - Detailed compound information with structure, target, activity, IC50 value, and biological activity description; - Structurally diverse, medicinally active, and cell permeable; - NMR and HPLC validated to ensure high purity and quality. Uses: Scientific use. Product Category: L2500. Categories: Human Endogenous Metabolite Libraries. |  |
| human endogenous retrovirus K endopeptidase | In peptidase family A2. Group: Enzymes. Synonyms: human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Enzyme Commission Number: EC 3.4.23.50. 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-4288; human endogenous retrovirus K endopeptidase; EC 3.4.23.50; human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Cat No: EXWM-4288. |  |
| 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 Factor XI | Factor XI is a plasma glycoprotein which circulates in a non-covalent complex with high molecular weight kininogen. The mature molecule is synthesized in the liver and is a two-chain homodimer with a molecular weight of approximately 160,000. It is estimated that 5% of the total mass is attributable to carbohydrate. The two identical monomers have molecular weights of 80,000, and are joined together by disulfide bonds. Thus by SDS-PAGE analysis, factor XI appears as a single band both non-reduced (Mr=160,000), and reduced (Mr=80,000).Factor XI circulates as a zymogen and requires proteolytic activation to acquire serine protease activity. The conversion of factor XI to factor XIa is ...activity or antigen levels. This latter observation may be related to the ability of the tissue factor/factor VIIa complex to also activate factor IX to IXa.Historically, factor XI has been difficult to purify due to its relatively low concentration in plasma, and its susceptibility to proteolysis. Factor XI is purified from fresh frozen plasma that is stabilized by added inhibitors. The plasma is first treated with BaCl2 to remove the vitamin K-dependent proteins, and factor XI is then isolated by affinity chromatography. A final chromatography step on heparin sepharose yields a homogeneous preparation of intact factor XI. The finished product is supplied in 50% (vol/vol) glycerol/H2 | |
| Human Factor XII | Factor XII (XII) (Hageman Factor) is a single chain (Mr=78,000) glycoprotein zymogen that circulates in plasma at a concentration of 40 ug/ml. Reciprical activation of XII to the active serine protease factor XIIa (XIIa) by kallikrein is central to initiation of the intrinsic coagulation pathway. Surface bound α-XIIa in turn activates factor XI to XIa. Secondary cleavage of α-XIIa by kallikrein yields β-XIIa, which catalyzes solution phase activation of kallikrein, factor VII and the classical complement cascade.The ability of a variety of negatively charged substances, both physiological and nonphysiological to promote XII activation and, thus, initiation of the int...ain (Mr=28,000) contains the catalytic triad (His-40, Asp-89, Ser-191), while the NH2-terminal heavy chain (Mr=52,000) conatins the anionic surface binding portion of the molecule. A secondary cleavage of α-XIIa by kallikrein outside the disulfide bond yields β-XIIa (XIIf, BHFa, HFf, hageman factor fragments) (Mr=28,000), which no longer binds anionic surfaces. β-XIIa can activate prekallikrein, but has little procoagulant activity. Several other minor intermediate forms of XIIa are indicated in the figure above.Inhibitors of XIIa include C1-INH, α2-antiplasmin, α2-macroglobulin and antithrombin III. At physiological concentrations, the relative effectiven | |
| Human Factor XIII | Factor XIII is the zymogenic form of the glutaminyl-peptide g-glutamyl transferase factor XIIIa (fibrinoligase, plasma transglutaminase, fibrin stabilizing factor, E.C. 2.3.2.13). Factor XIII is unique among transamidases in that it is a zymogen in vivo. Factor XIII is found both extracellularly in plasma and intracellularly in platelets, megakaryocytes, monocytes, placenta, uterus, liver and prostrate tissues. Plasma factor XIII is synthesized in the liver and circulates as a tetramer (Mr=320,000), composed of 2 pairs of nonidentical subunits (A2B2). The intra-cellular forms are synthesized in the tissues where they reside as dimers (Mr=146,000) of 2 identical A chains (A2). The A ...nly after the Ca2+ (Kd=10-3M) and fibrin(ogen) (Kd=10-8M) dependent dissociation of the B subunit dimer from the A2' dimer.In the coagulation cascade, factor XIIIa functions to stabilize the fibrin clot by crosslinking the a and g-chains of fibrin. Other proteins known to be substrates for Factor XIIIa which may be hemostatically important include fibronectin, α2-antiplasmin, collagen, factor V, von Willebrand Factor and thrombospondin.Factor XIII is purified from fresh frozen human plasma by a modification of the procedures described by Folke and Lorand involving barium citrate, ammonium sulfate and glycine precipitations, ion exchange chromatography and gel filtration. Factor | |
| human GIP(3-30), amide | Human GIP(3-30), amide is a high affinity antagonist of the human GIP receptor in vitro. Human GIP(3-30), amide has potential anti-obesity and anti-diabetic effects[1][2]. Uses: Scientific research. Group: Peptides. CAS No. 1884226-05-4. Pack Sizes: 5 mg; 10 mg. Product ID: HY-P10138. |  |
| human GIP(3-30), amide TFA | Human GIP(3-30), amide TFA is the TFA salt form of human GIP(3-30), amide (HY-P10138). Human GIP(3-30), amide TFA is a high affinity antagonist of the human GIP receptor in vitro. Human GIP(3-30), amide TFA has potential anti-obesity and anti-diabetic effects[1][2]. Uses: Scientific research. Group: Peptides. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P10138A. | |
| 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 hair (trace elements) | certified Reference Material. Group: Certified reference materials (crms). |  |
| Human Histatin 2 | Histatin 2 is a degradation product of histatin 1. It shows antibacterial and antifungal activity. Synonyms: H-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Glu-Phe-Pro-Phe-Tyr-Gly-Asp-Tyr-Gly-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn-OH. Grade: 97.4%. Molecular formula: C158H211N45O44. Mole weight: 3444.6. | |
| Human Histatin 4 | Human Histatin 4 is an antibacterial peptide isolated from Homo sapiens. It shows antibacterial and antifungal activity. Synonyms: H-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn-OH. Grade: 96.8%. Molecular formula: C121H174N42O33. Mole weight: 2744.9. | |
| Human Histatin 6 | Human Histatin 6 is an antibacterial peptide isolated from Homo sapiens. It shows antibacterial and antifungal activity. Synonyms: Asp-Ser-His-Ala-Lys-Arg-His-His-Gly-Tyr-Lys-Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg. Grade: 96.0%. Molecular formula: C139H207N55O34. Mole weight: 3192.4. | |
| Human Histatin 7 | Human Histatin 7 is an antibacterial peptide isolated from Homo sapiens. It shows antibacterial and antifungal activity. Synonyms: Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr. Grade: 97.8%. Molecular formula: C76H111N29O18. Mole weight: 1718.8. | |
| Human Histatin 8 | Human Histatin 8 is an antibacterial peptide isolated from Homo sapiens. It shows antibacterial and antifungal activity. Synonyms: Histatin-8; H-Lys-Phe-D-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-OH. Grade: 95.7%. CAS No. 127637-03-0. Molecular formula: C70H99N25O17. Mole weight: 1562.7. | |
| Human histatin 9 | Human Histatin 9 is an antibacterial peptide isolated from Homo sapiens. It shows antibacterial and antifungal activity. Synonyms: Arg-Lys-Phe-His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg. Grade: 95.9%. Molecular formula: C82H123N33O19. Mole weight: 1875.1. | |
| Human IgG1(D356E/L358M) kappa, Isotype Control | Human IgG1(D356E/L358M) kappa, Isotype Control, a human-derived monoclonal antibody, is an isotype control for human IgG1(D356E/L358M)? antibody[1]. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P990100. | |
| Human IgG1 (K214R) kappa, Isotype Control | Human IgG1 (K214R) kappa, Isotype Control, a human-derived antibody, is an isotype control for human IgG1 (K214R)? antibody. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P99995. | |
| Human IgG1 kappa, Isotype Control | Human IgG1 kappa, Isotype Control is a human monoclonal antibody that is the isotype control of human IgG1 kappa antibody[1]. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg. Product ID: HY-P99001. | |
| Human IgG1 lambda1, Isotype Control | Human IgG1 lambda1, Isotype Control, a human-derived antibody, is an isotype control for human IgG1?1 antibody. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P99992. | |
| Human IgG1 lambda2, Isotype Control | Human IgG1 lambda2, Isotype Control is a human monoclonal antibody that is the isotype control of human IgG1? antibody. Isotype control antibodies can help remove non-specific signals from experimental results and assess the accuracy and reliability of the experiment[1]. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P990096. | |
| Human IgG1 (N297A) kappa, Isotype Control | Human IgG1 (N297A) kappa, Isotype Control, a human-derived antibody, is an isotype control for human IgG1 (N297A)? antibody. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P99994. | |
| Human IgG2 kappa, Isotype Control | Human IgG2 kappa, Isotype Control, a human monoclonal antibody, is an isotype control for human IgG2? antibody[1]. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 500 ?g; 1 mg; 5 mg; 10 mg. Product ID: HY-P99002. | |
| Human IgG4 (S228P) kappa, Isotype Control | Human IgG4 (S228P) kappa, Isotype Control, a human-derived monoclonal antibody, is an isotype control for human IgG4? antibody. Uses: Scientific research. Group: Inhibitory antibodies. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P99003. | |
| Human IgG?Agarose | saline suspension. Group: Fluorescence/luminescence spectroscopy. | |
| Human immunoglobulin for anticomplementary activity | Human immunoglobulin for anticomplementary activity. Uses: For analytical and research use. Group: European pharmacopoeia (ph. eur.); pharmacopoeial standards. Alternative Names: Human normal immunoglobulin for intravenous administration, ?-Blood globulins,?-Globulins, ?-Globulin, Globulins, ?-globulin, Blood plasma ?-globulins, Globulin, blood, ?-, Plasma ?-globulins, Human normal immunoglobulin, Gamma globulins, Globulin, blood, gamma-, Intacglobin, Blood gamma-globulin, Human normal immunoglobulin, Gamma- blood globulin, Globulins, ?-, conjugates, Globulins, blood-serum ?-, Globulins, ?-, Globulins, blood serum, ?-, Gamma globulin, Gamma- blood globulins. CAS No. 9007-83-4. Catalog: APS9007834B. Format: Neat. Shipping: +5°C. | |
| Humanin | Humanin. Synonyms: Protein Humanin (human). Grade: ≥95%. CAS No. 330936-69-1. Molecular formula: C119H204N34O32S2. Mole weight: 2687.22. | |
| Humanin | Humanin, an anti-apoptotic peptide of 24 amino acids, is a Bax inhibitor. Humanin prevents the translocation of Bax from cytosol to mitochondria, blocks Bax from the inactive to active conformation. Humanin is a mitochondria-associated peptide with a neuroprotective effect against AD-related neurotoxicity. Humanin also improves overall insulin sensitivity in animal. Humanin are related to aging [1] [2]. Humanin analogue, in which the serine at position 14 is replaced by glycine, names HNG [2]. Uses: Scientific research. Group: Peptides. CAS No. 330936-69-1. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-P1928. | |
| Humanin (human) (trifluoroacetate salt) | Humanin is a micropeptide encoded by the 16S ribosomal RNA gene MT-RNR2 in the mitochondrial genome. Synonyms: H-Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala-OH.TFA; L-methionyl-L-alanyl-L-prolyl-L-arginyl-glycyl-L-phenylalanyl-L-seryl-L-cysteinyl-L-leucyl-L-leucyl-L-leucyl-L-leucyl-L-threonyl-L-seryl-L-alpha-glutamyl-L-isoleucyl-L-alpha-aspartyl-L-leucyl-L-prolyl-L-valyl-L-lysyl-L-arginyl-L-arginyl-L-alanine trifluoroacetic acid. Grade: 95%. Molecular formula: C121H205F3N34O34S2. Mole weight: 2801.3. | |
| Human Kininogen (Single Chain High Molecular Weight) | High Molecular Weight Kininogen (HK) is a non-enzymatic cofactor of the contact activation system. HK is thought to have two functions in the contact activation system. First, HK links Prekallikrein to a negatively charged surface thereby allowing activation of Kallikrein by surface bound Factor a-XIIa. HK also forms a complex with Factor XI and accelerates its activation to XIa by a-XIIa. Additionally HK serves as a source of Bradykinin, a potent vasoactive peptide important in hypotension studies. The protein purity is determined by SDS-PAGE. Group: Zymogens. Purity: >95% by SDS-PAGE. Kininogen. Mole weight: 120000. Storage: 2-8°C. Source: Human. Human Kininogen (Single Chain High Molecular Weight); Kininogen. Pack: 1mg. Cat No: CZY-028. | |
| Human Kininogen (Two Chain High Molecular Weight) | ERL offers the two chain Kinin-free form of Kininogen. This is prepared by Kallikrein digestion of Kininogen which is then repurified to remove traces of Kallikrein. Group: Zymogens. Purity: >95% by SDS-PAGE. Kininogen. Mole weight: 110000. Storage: 2-8°C. Source: Human. Human Kininogen (Two Chain High Molecular Weight); Kininogen. Pack: 1mg. Cat No: CZY-029. | |
| Human KR-20 | Human KR-20 is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria and fungi. Synonyms: Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser. Molecular formula: C109H190N36O29. Mole weight: 2468.93. | |
| Human KS-27 | Human KS-27 is an antibacterial peptide isolated from Homo sapiens. Synonyms: Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg. Grade: 96.2%. Molecular formula: C151H261N47O37. Mole weight: 3327.03. | |
| Human KS-30 | Human KS-30 is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria and fungi. Synonyms: Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser. Molecular formula: C163H280N50O44. Mole weight: 3644.32. | |
| Human lactoferricin | Human lactoferricin is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria and gram-negative bacteria. Synonyms: hLF(21-31); Phe-Gln-Trp-Gln-Arg-Asn-Met-Arg-Lys-Val-Arg. Grade: 96.2%. Molecular formula: C247H402N74O59S5. Mole weight: 1,567. | |
| Human LL-23 | Human LL-23 is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria and fungi. Synonyms: Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg. Grade: 96.1%. Molecular formula: C130H216N38O32. Mole weight: 2823.38. | |
| Human LL-29 | Human LL-29 is an antibacterial peptide isolated from Homo sapiens. Synonyms: Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg. | |
| 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 Metabolite Library | A unique collection of 4532 human metabolites for high-throughput, high-content screening. - An effective tool for studying human metabolic diseases, exploring the pathogenesis of cancer and finding new drugs. - Some compounds have been marketed or entered the clinical phase, which ensured low bio-toxicity and high bio-activity. - Structural diversity, significant drug potency and cell permeability. - Detailed specifications, description of compound structures, activity, etc. - Various detection techniques such as NMR, HPLC/LCMS to ensure correct structure and high purity of the product and reduce false positives. Uses: Scientific use. Product Category: L2570. Categories: Human Metabolite Libraries. | |
| Human Microsomal Transfer Protein (MTP) | Supplied by Roar Biomedical, Inc. Group: Fluorescence/luminescence spectroscopy. | |
| Human milk lysozyme | Human milk lysozyme is the lysozyme found in human milk. Human milk lysozyme is thought to be a key defense factor in protecting the gastrointestinal tract of newborns against bacterial infection [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 12671-19-1. Pack Sizes: 100 mg; 250 mg; 500 mg; 1 g. Product ID: HY-P3021. | |
| Human MUC7 20-Mer | Human MUC7 20-Mer is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria and fungi. Synonyms: Leu-Ala-His-Gln-Lys-Pro-Phe-Ile-Arg-Lys-Ser-Tyr-Lys-Cys-Leu-His-Lys-Arg-Cys-Arg. Grade: 97.6%. Molecular formula: C112H186N38O24S2. Mole weight: 2513.07. | |
| Human neutrophil peptide-1 | Human neutrophil peptide-1 is an antimicrobial peptide found in Homo sapiens (Human). It belongs to the alpha-defensin family and has antimicrobial activity against gram-negative bacteria, gram-positive bacteria and Fungi. Synonyms: H-Ala-Cys(1)-Tyr-Cys(2)-Arg-Ile-Pro-Ala-Cys(3)-Ile-Ala-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys(2)-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys(3)-Cys(1)-OH; L-alanyl-L-cysteinyl-L-tyrosyl-L-cysteinyl-L-arginyl-L-isoleucyl-L-prolyl-L-alanyl-L-cysteinyl-L-isoleucyl-L-alanyl-glycyl-L-alpha-glutamyl-L-arginyl-L-arginyl-L-tyrosyl-glycyl-L-threonyl-L-cysteinyl-L-isoleucyl-L-tyrosyl-L-glutaminyl-glycyl-L-arginyl-L-leucyl-L-tryptophyl-L-alanyl-L-phenylalanyl-L-cysteinyl-L-cysteine (2->30),(4->19),(9->29)-tris(disulfide); Human Defensin NP-1; alpha-Defensin-1; Defensin HNP-1 (human); HNP-1; Defensin human neutrophil peptide-1. Grade: >95%. CAS No. 99287-08-8. Molecular formula: C150H222N44O38S6. Mole weight: 3442.03. | |
| Human neutrophil peptide-2 | Human neutrophil peptide-2 is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria, fungi and viruses. Synonyms: Neutrophil Peptide-2; Defensin HNP-2 human; Defensin HNP-2; alpha-Defensin-2; H-Cys(1)-Tyr-Cys(2)-Arg-Ile-Pro-Ala-Cys(3)-Ile-Ala-Gly-Glu-Arg-Arg-Tyr-Gly-Thr-Cys(2)-Ile-Tyr-Gln-Gly-Arg-Leu-Trp-Ala-Phe-Cys(3)-Cys(1)-OH. Grade: 95.2%. CAS No. 99287-07-7. Molecular formula: C147H217N43O37S6. Mole weight: 3371.0. | |
| Human Papillomavirus (HPV) E7 protein (49-57) | Human Papillomavirus (HPV) E7 protein (49-57) is the H-2 d -restricted human papillomavirus (HPV) E7 49-57 epitope (short peptide spanning the 49th to 57th amino acid residues in the E7 protein) [1]. Uses: Scientific research. Group: Peptides. CAS No. 151812-18-9. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P1907. | |
| Human Papillomavirus (HPV) E7 protein 49-57 | It is a H-2d-restricted human papillomavirus (HPV) E749-57 epitope. Synonyms: H-Arg-Ala-His-Tyr-Asn-Ile-Val-Thr-Phe-OH; L-arginyl-L-alanyl-L-histidyl-L-tyrosyl-L-asparagyl-L-isoleucyl-L-valyl-L-threonyl-L-phenylalanine. Grade: ≥95%. CAS No. 151812-18-9. Molecular formula: C52H77N15O13. Mole weight: 1120.26. | |
| Human PD-L1 inhibitor I | Human PD-L1 inhibitor I is a hPD-1 peptide ligand, with a K D of 3.39 μM. Human PD-L1 inhibitor I may disturb the binding of hPD-L1 to hPD-1 [1]. Uses: Scientific research. Group: Peptides. CAS No. 2135542-86-6. Pack Sizes: 5 mg; 10 mg. Product ID: HY-P2474. | |
| Human PD-L1 inhibitor V | Human PD-L1 inhibitor V is a competitive human PD-1 protein inhibitor. Molecular formula: C65H104N20O18S. Mole weight: 1485.71. | |
| Human Prekallikrein | Purified from fresh frozen human plasma. Human Prekallikrein is a single chain gamma globulin glycoprotein that participates in the early phase of contract activation, kinin formation and fibrinolysis. Prekallikrein purity is determined by SDS-PAGE and shows no reduction upon incubation with 2-mercaptoethanol. Activity is determined via clotting assay. Group: Zymogens. Purity: >95% by SDS-PAGE. Prekallikrein. Mole weight: 86000. Storage: 2-8°C. Source: Human. Human Prekallikrein; Prekallikrein. Pack: 1mg. Cat No: CZY-027. | |
| 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 | |
| Human PTHrP-(1-36) | Human PTHrP-(1-36) is a secretory form of PTHrP with anticalciuric effects. Human PTHrP-(1-36) enhances beta cell function and proliferation. Human PTHrP-(1-36) can be used in the research of humoral hypercalcemia of malignancy (HHM) and hyperparathyroidism[1][3]. Uses: Scientific research. Group: Peptides. CAS No. 172867-62-8. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-106288. | |
| Human RK-31 | Human RK-31 is an antibacterial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria, gram-negative bacteria and fungi. Synonyms: Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser. Molecular formula: C169H292N54O45. Mole weight: 3800.51. | |
| Human salvic | Human salvic is a cyclic antimicrobial peptide isolated from Homo sapiens. It has activity against gram-positive bacteria and gram-negative bacteria. Synonyms: Met-His-Asp-Phe-Trp-Val-Leu-Trp-Val-Leu-Leu-Glu-Tyr-Ile-Tyr-Asn-Ser-Ala-Cys-Ser-Val-Leu-Ser-Ala-Thr-Ser-Ser-Val-Ser-Ser-Arg-Val-Leu-Asn-Arg-Ser-Leu-Gln-Val-Lys-Val-Val-Lys-Ile-Thr-Asn. | |
| Human serum (17?-estradiol, high level) | certified Reference Material. Group: Certified reference materials (crms). | |
| Human serum (17?-estradiol, low level) | certified Reference Material. Group: Certified reference materials (crms). | |
| Human serum (17?-estradiol, medium level) | certified Reference Material. Group: Certified reference materials (crms). | |
| Human serum albumin | Human serum albumin (HSA) is the most abundant protein in plasma and is a major determinant of plasma oncotic pressure. Human serum albumin exhibits antioxidant, anticoagulant, anti-inflammatory, anti-platelet aggregation activities as well as colloid osmotic action. Human serum albumin can block the inhibitory effect of GML on human T cells, providing protective function for T cells. Human serum albumin is also associated with cardiovascular diseases and can partially prevent the LPS (HY-D1056) induced oxidative stress, as well as the upregulation of NF-κB , NF-κB , and peroxynitrite (ONOO - ) in the vascular wall, contributing to the reduction of blood pressure [1] [2] [3]. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: HSA. CAS No. 70024-90-7. Pack Sizes: 100 mg; 250 mg; 500 mg; 1 g; 1 mg. Product ID: HY-P1956. | |
| Human Serum Albumin | H S A. CAS No. 70024-90-7. Product ID: 8-01713. Molecular formula: C2936H4624N786O889S41. Mole weight: 66,478 Da. Purity: 97-99%. Properties: [a]D -20- -23º mp 106-109 ºC toxic solid. |  |
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