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| Product | Description | |
|---|---|---|
| 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 | |
| α-epidermal growth factor, human | Recombinant human epidermal growth factor has the same structure as the human epidermal growth factor. EGF binds to epidermal growth factor receptor (EGFR) and stimulates cell growth and proliferation. Recombinant human epidermal growth factor is approved for the treatment of diabetic foot ulcers. Uses: The treatment of diabetic foot ulcers. Synonyms: Human EGF; Nepidermin. CAS No. 62253-63-8. Molecular formula: C270H401N73O83S7. Mole weight: 6222. |  |
| Atrial natriuretic factor (1-28) (human, porcine) | Atrial natriuretic factor (1-28) (human, porcine) is a 28 amino acid peptide corresponding to the rat protein sequence. It is an endogenous peptide synthesized in myoendocrine cells of the heart from which it is released into the circulation. It has effects on the renal and cardiovascular systems that decrease vasoconstriction, increase sodium excretion and inhibit renin secretion. It decreases plasma renin activity and cAMP levels in anesthetized rats and increases cGMP levels at 8 μg/kg. It also inhibits arginine vasopressin-induced increase in mean arterial blood pressure in spontaneously hypertensive and control rats when administered intracerebroventricularly at a dose of 150 ng. It produces diuretic, natriuretic and vasodilatory effects through stimulation of guanylate cyclase-linked NPR-A receptors. It plays an important role in blood volume and blood pressure regulation. Synonyms: ANF 1-28; hANF; Atrial Natriuretic Peptide human. CAS No. 91917-63-4. Molecular formula: C127H205N45O39S3. Mole weight: 3080.46. | |
| Atrial Natriuretic Factor (5-27) (human) | Synonyms: Atrial Natriuretic Peptide-23 (human); H-Ser-Ser-Cys-Phe-Gly-Gly-Arg-Met-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-Asn-Ser-Phe-Arg-OH (Disulfide bridge: Cys3-Cys19); L-seryl-L-seryl-L-cysteinyl-L-phenylalanyl-glycyl-glycyl-L-arginyl-L-methionyl-L-alpha-aspartyl-L-arginyl-L-isoleucyl-glycyl-L-alanyl-L-glutaminyl-L-seryl-glycyl-L-leucyl-glycyl-L-cysteinyl-L-asparagyl-L-seryl-L-phenylalanyl-L-arginine (3->19)-disulfide. Grades: ≥95%. CAS No. 98929-56-7. Molecular formula: C97H154N34O32S3. Mole weight: 2404.67. | |
| COAGULATION FACTOR XII, HUMAN | COAGULATION FACTOR XII, HUMAN. Uses: Designed for use in research and industrial production. Additional or Alternative Names: HUMAN PLASMA ACTIVATED HAGEMAN FACTOR;HUMAN PLASMA FACTOR XII;HUMAN PLASMA FACTOR XIIA;HUMAN PLASMA HAGEMAN FACTOR;HAGEMAN FACTOR, HUMAN;FACTOR XIIA, HUMAN;FACTOR XII (HUMAN);COAGULATION FACTOR XII, HUMAN. Product Category: Heterocyclic Organic Compound. CAS No. 9001-30-3. Product ID: ACM9001303. Alfa Chemistry ISO 9001:2015 Certified. |  |
| COAGULATION FACTOR XIII, HUMAN | COAGULATION FACTOR XIII, HUMAN. Uses: Designed for use in research and industrial production. Additional or Alternative Names: FIBRIN-STABILIZING FACTOR;FIBRIN-STABILIZING FACTOR, HUMAN;FACTOR XIII (HUMAN);HUMAN PLASMA FACTOR XIII;COAGULATION FACTOR XIII, HUMAN;COAGULATION FACTOR XIII, HUMAN PLASMA. Product Category: Heterocyclic Organic Compound. CAS No. 9013-56-3. Product ID: ACM9013563. Alfa Chemistry ISO 9001:2015 Certified. | |
| Complement factor D from human plasma | 90-110 ?g/mL in PBS, pH 7.2, ?90% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. |  |
| Complement factor H from human plasma | 1 mg/mL in PBS, pH 7.2, ?90% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Complement factor I from human plasma | >90% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| E2F Transcription Factor 6 human | histidine tagged, recombinant, expressed in E. coli. Group: Fluorescence/luminescence spectroscopy. | |
| ?-Endothelial Cell Growth Factor human | ?-ECGF, recombinant, expressed in E. coli, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Epidermal Growth Factor, human (hEGF) | recombinant (E. coli). Group: Fluorescence/luminescence spectroscopy. | |
| Epidermal Growth Factor Receptor human | lyophilized powder, ?15,000 units/mg protein (Bradford). Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor-10 human | >97% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor-18 human | >95% (SDS-PAGE and HPLC), recombinant, expressed in E. coli, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| FIBROBLAST GROWTH FACTOR-4 HUMAN RECOMBI | FIBROBLAST GROWTH FACTOR-4 HUMAN RECOMBI. Uses: Designed for use in research and industrial production. Additional or Alternative Names: FIBROBLAST GROWTH FACTOR-4 HUMAN RECOMBI;fibroblast growth factor-4 human*recombinant cell;FIBROBLAST GROWTH FACTOR-4, HUMAN RECOMB INANT, CELL CULTURE TESTED. Product Category: Heterocyclic Organic Compound. CAS No. 123584-45-2. Product ID: ACM123584452. Alfa Chemistry ISO 9001:2015 Certified. | |
| Fibroblast Growth Factor-5 human | recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture, ?97% (SDS-PAGE and N-terminal analysis). Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor-9 human | recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder, suitable for cell culture, ?97% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor-Acidic human | FGF-Acidic, recombinant, expressed in E. coli, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor-Basic Heparin Stabilized human | FGF-Basic, recombinant, expressed in E. coli, sterile-filtered, aqueous solution, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Fibroblast Growth Factor Receptor-2? (IIIc)/Fc Chimera human | >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Glial Cell Line-derived Neurotrophic Factor human | recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture, ?98% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Granulocyte colony-stimulating factor human | G-CSF, recombinant, expressed in E. coli, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Granulocyte-Macrophage Colony-Stimulating Factor human | GM-CSF, Animal-component free, recombinant, expressed in E. coli, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Granulocyte-Macrophage Colony-Stimulating Factor human | GM-CSF, recombinant, expressed in E. coli, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Heat Shock Factor 1 human | recombinant, expressed in E. coli, ~65% (SDS-PAGE), solution. Group: Fluorescence/luminescence spectroscopy. | |
| Heparin-Binding EGF-Like Growth Factor human | HB-EGF, recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Hepatocyte Growth Factor human | HGF, recombinant, expressed in Baculovirus infected High-5 cells, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Hepatocyte Growth Factor human | HGF, recombinant, expressed in NSO cells, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Hepatocyte Growth Factor Receptor (c-Met)/Fc Chimera human | >95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Human Coagulation Factor VII | Human factor VII is a single chain, vitamin K-dependent, plasma glycoprotein which is synthesized in the liver. Prior to secretion into the blood, post translational modification by a vitamin K-dependent carboxylase produces ten-carboxyglutamic acid (gla) residues located in the NH2-terminal portion of the molecule, which facilitate cell membrane binding. Factor VII is proteolytically activated to the serine protease, factor VIIa, during coagulation. Factor VII can be activated by thrombin, factor IXa, factor Xa or factor XIIa. The activation results in cleavage of the single chain molecule on the COOH-terminal side of arginine-152, to produce an NH2-terminal derived light chai...nzyme complex catalyzes the conversion of both factor IX to factor IXa and factor X to factor Xa. The cDNA for factor VII has been isolated and the nucleotide sequence determined. Factor VII shares extensive sequence homology with other serine proteases including factor IX, factor X and protein C.Human factor VII is purified using a combination of conventional techniques and immunoaffinity chromatography. The purified protein is supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured in a factor VII clotting assay. Group: Zymogens. CAS No. 9001-25-6. Purity: >95% by SDS-PAGE. Factor VII. Mole weigh | |
| Human 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 | |
| Hypercalcemia of malignancy factor fragment 1-34 amide human | Hypercalcemia of malignancy factor fragment 1-34 amide is an extraordinary biomedical innovation exhibiting remarkable potential in the research of hypercalcemia linked to malignancies. Synonyms: Hypercalcemia of Malignancy Factor (1-34) amide (human, mouse, rat); H-Ala-Val-Ser-Glu-His-Gln-Leu-Leu-His-Asp-Lys-Gly-Lys-Ser-Ile-Gln-Asp-Leu-Arg-Arg-Arg-Phe-Phe-Leu-His-His-Leu-Ile-Ala-Glu-Ile-His-Thr-Ala-NH2; pTH-Related Protein (1-34) amide (human, mouse, rat); L-alanyl-L-valyl-L-seryl-L-alpha-glutamyl-L-histidyl-L-glutaminyl-L-leucyl-L-leucyl-L-histidyl-L-alpha-aspartyl-L-lysyl-glycyl-L-lysyl-L-seryl-L-isoleucyl-L-glutaminyl-L-alpha-aspartyl-L-leucyl-L-arginyl-L-arginyl-L-arginyl-L-phenylalanyl-L-phenylalanyl-L-leucyl-L-histidyl-L-histidyl-L-leucyl-L-isoleucyl-L-alanyl-L-alpha-glutamyl-L-isoleucyl-L-histidyl-L-threonyl-L-alaninamide; PTHrP (1-34) amide. Grades: 95%. CAS No. 112955-31-4. Molecular formula: C180H288N58O47. Mole weight: 4016.57. | |
| Insulin-Like Growth Factor Binding Protein-2 human | recombinant, expressed in NSO cells, lyophilized powder, suitable for cell culture, ?95% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-Like Growth Factor Binding Protein-3 human | recombinant, expressed in NSO cells, lyophilized powder, suitable for cell culture, ?95% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-like Growth Factor Binding Protein-5 human | >90% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-like Growth Factor-I (E3R) human | >95% (HPLC), recombinant, expressed in E. coli, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-like Growth Factor-I human | IGF-I, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-like Growth Factor-II human | IGF-II, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Insulin-like Growth Factor-I Receptor human | ?95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Keratinocyte Growth Factor human | KGF, recombinant, expressed in E. coli, powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Leukemia Inhibitory Factor human | LIF, recombinant, expressed in E. coli, 10 ?g/ml, buffered aqueous solution (pH 7.4), suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Macrophage Colony-Stimulating Factor human | M-CSF, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Myc-associated factor X (MAX) human | recombinant, expressed in E. coli, ?80% (SDS-PAGE). Group: Fluorescence/luminescence spectroscopy. | |
| Native Human Factor α-XIIa | Human Factor α-XIIa is a serine protease responsible for the activation of Factor XI to XIa in the contact activation system. Human Factor XII and prekallikrein are thought to be involved in a reciprocal activation mechanism in which Factor XIIa activates prekallikrein to kallikrein, which in turn converts Factor XII to XIIa. Factor XIIa activates Factor XI to XIa thereby triggering the Contact Factor cascade. ERL offers Factor α-XIIa which is activated by the autoactivation process with Dextran Sulfate and re-purified to remove the activator. The protein purity is determined by SDS-PAGE and activity is determined via clotting assay. Group: Enzymes. Synonyms: Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Factor α-XIIa. Mole weight: 80 kDa. Activity: 69.51 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Cat No: NATE-0882. | |
| Native Human Factor IXa β | Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa&beta. Group: Enzymes. Synonyms: Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Factor IXa Beta. Mole weight: 45 kDa. Activity: 12500.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Cat No: NATE-0883. | |
| Native Human Factor VIIa | Prepared from purified Human Factor VII using Human Factor XIIa. The Factor Xlla is removed using affinity chromatography. Purity is determined by SDS-PAGE. Human Factor VIIa reduces to 29,500 and 23,500 with the addition of 2-mercaptoethanol. Activity is determined via clotting assay. Factor Vlla, in the presence of calcium ions and Tissue factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa. Group: Enzymes. Synonyms: Human Factor VII; Factor VII. Factor VIIa. Mole weight: 50 kDa. Activity: 53833.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor VII; Factor VII. Cat No: NATE-0884. | |
| Native Human Factor Xa | Human Factor Xa is prepared from Human Factor X by activation with Russell's Viper Venom. This RVV-X is removed after activation. Complete activation is observed by SDS-PAGE. Factor Xa along with cofactor Va, phospholipids and calcium ions, (the prothrombinase complex) catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Human Factor Xa; Factor Xa. Factor Xa. Mole weight: 46 kDa. Activity: 218.00 IU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Xa; Factor Xa. Cat No: NATE-0885. | |
| Native Human Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Human Factor XIIIa | Human Factor XIII is cleaved with human alpha thrombin. The thrombin is subsequently removed via chromatography. The above protein was purified from Human plasma that was tested and found negative by FDA accepted methods fro Anti-HIV1/2, Anti-HTLV I & II, HBsAg, Anti-HCV, Syphilis, ABC ab, HIV-1 p24 Ag or HIV-1 RNA, HCV RNA and HBV RNA. Donors are screened for CJD (Creutzfeldt-Jakob Disease). Group: Enzymes. Synonyms: Human Factor XIIIa; Factor XIIIa. Factor XIIIa. Mole weight: 312 kDa. Activity: 1968.00 Loewy u/mg. Storage: -20°C. Source: Human. Species: Human. Human Factor XIIIa; Factor XIIIa. Cat No: NATE-0887. | |
| Nerve Growth Factor Receptor/Fc Chimera human | >95% (SDS-PAGE), recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder. Group: Fluorescence/luminescence spectroscopy. | |
| Placenta Growth Factor human | PlGF, recombinant, expressed in E. coli, powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Platelet-Derived Endothelial Cell Growth Factor human | recombinant, expressed in baculovirus infected Sf21 cells, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Platelet-Derived Growth Factor-AA human | PDGF-AA, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Platelet-Derived Growth Factor-AB human | PDGF-AB, recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Platelet Factor 4 (58-70), human | It is the 58-70 amino acid fragment of Platelet Factor 4 (PF-4) that contains the major heparin-binding domain and is insufficient to fully exert its antiangiogenic activity. Synonyms: PF4 (58-70) (human); Pro-Leu-Tyr-Lys-Lys-Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser; L-prolyl-L-leucyl-L-tyrosyl-L-lysyl-L-lysyl-L-isoleucyl-L-isoleucyl-L-lysyl-L-lysyl-L-leucyl-L-leucyl-L-alpha-glutamyl-L-serine; platelet factor 4 fragment 58-70 human. Grades: 95%. CAS No. 82989-21-7. Molecular formula: C76H133N17O18. Mole weight: 1572.97. | |
| Prepro-Atrial Natriuretic Factor (26-55) (human) | Prepro-Atrial Natriuretic Factor (26-55) (human) is a polypeptide that increases renal cortical and medullary cyclic GMP levels. Prepro-Atrial Natriuretic Factor (26-55) (human) increases renal guanylate cyclase activity [1]. Uses: Scientific research. Group: Peptides. CAS No. 112160-82-4. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P4811. |  |
| Prepro-Atrial Natriuretic Factor (26-55) (human) | Prepro-Atrial Natriuretic Factor (human) can reduce adenylate cyclase activity. Synonyms: PREPRO-HANF (26-55) CARDIODILATIN-RELATED PEPTIDE (HUMAN); PREPRO-HANF FRAGMENT 26-55, HUMAN; PREPRO-ANF (26-55), HUMAN; PREPRO-ATRIAL NATRIURETIC FACTOR (26-55) (HUMAN); PREPRO-ATRIAL NATRIURETIC PEPTIDE, FRAGMENT 26-55 HUMAN; H-ASN-PRO-MET-TYR-ASN-ALA-VAL-S. Grades: 95%. CAS No. 112160-82-4. Molecular formula: C152H236N38O51S3. Mole weight: 3507.92. | |
| rec Brain-Derived Neurotrophic Factor (human) | Brain-derived neurotrophic factor (BDNF), a member of the neurotrophin family, has its expression in the human central nervous system and is altered in neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. It promotes the survival of dopaminergic neurons and protects against Aβ-induced neurotoxicity in vivo and in vitro. Synonyms: rec BDNF (human). | |
| Recombinant human epidermal growth factor | rhEGF, human Oligopeptide-1. antirheumatic. CAS No. 62253-63-8. Product ID: 8-01731. Purity: 98% activity 6*105IU/mg. Source : |  |
| Rheumatoid Factor, Control Serum, Human | Rheumatoid arthritis (RA) is a chronic inflammatory disease of unknown etiology. Rheumatoid arthritis is a systemic disease characterized by chronic proliferation and inflammation of joint cartilage and supporting structures. RA is mainly defined by clinical criteria, in which systematic pathogenetic studies have been hampered by doubts about the presence of common pathogenetic mechanisms and the relative lack of unique laboratory findings. IgG rheumatoid factor has been reported to be present in sera of patients with rheumatoid arthritis both with and without IgM rheumatoid factor activity. Group: Biologicals. Grades: Serum. Pack Sizes: 2ml. US Biological Life Sciences. |  Worldwide |
| Stem Cell Factor human | SCF, recombinant, expressed in E. coli, powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Stromal Cell-Derived Factor 1?/pre-B Cell Growth Stimulating Factor human | >97% (SDS-PAGE), recombinant, expressed in E. coli, lyophilized powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Transforming Growth Factor-?1 from human platelets | TGF-?1, lyophilized powder, suitable for cell culture, 1 × 106 U/mg. Group: Fluorescence/luminescence spectroscopy. | |
| Transforming Growth Factor-?1 human | TGF-?1, recombinant, expressed in CHO cells, powder, suitable for cell culture. Group: Fluorescence/luminescence spectroscopy. | |
| Transforming Growth Factor-?1, human (hTGF-?1) | recombinant (CHO cells). Group: Fluorescence/luminescence spectroscopy. | |
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