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| Product | Description | |
|---|---|---|
| Pancreatic polypeptide | Pancreatic polypeptide is a peptide secreted by the endocrine PP cells of the pancreas that regulates pancreatic secretory activity and also affects hepatic glycogen stores and gastrointestinal secretion [1]. Uses: Scientific research. Group: Peptides. CAS No. 59763-91-6. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P4060. |  |
| Pancreatic Polypeptide, bovine | Pancreatic Polypeptide, bovine, a straight chain polypeptide containing 36 amino acids, derived primarily from the pancreas, and stimulates pancreatic secretion by inhibiting secretin and cholecystokinin. As the NPY receptor agonist, it has a high affinity at NPYR4. Synonyms: Ala-Pro-Leu-Glu-Pro-Glu-Tyr-Pro-Gly-Asp-Asn-Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr-Ala-Ala-Glu-Leu-Arg-Arg-Tyr-Ile-Asn-Met-Leu-Thr-Arg-Pro-Arg-Tyr-NH2; Pancreatic polypeptide (pig), 6-L-glutamic acid-; Bovine pancreatic polypeptide. Grade: ≥95%. CAS No. 179986-89-1. Molecular formula: C186H287N53O56S2. Mole weight: 4225.78. |  |
| Pancreatic polypeptide(human) | Pancreatic polypeptide(human). Uses: Designed for use in research and industrial production. Additional or Alternative Names: PANCREATIC POLYPEPTIDE;PANCREATIC POLYPEPTIDE, HUMAN;PP, HUMAN;APLEPVYPGDNATPEQMAQYAADLRRYINMLTRPRY-NH2;H-ALA-PRO-LEU-GLU-PRO-VAL-TYR-PRO-GLY-ASP-ASN-ALA-THR-PRO-GLU-GLN-MET-ALA-GLN-TYR-ALA-ALA-ASP-LEU-ARG-ARG-TYR-ILE-ASN-MET-LEU-THR-ARG-PRO-ARG-TYR-NH2. Product Category: Heterocyclic Organic Compound. CAS No. 59763-91-6. Molecular formula: C185H287N53O54S2. Product ID: ACM59763916. Alfa Chemistry ISO 9001:2015 Certified. |  |
| Pancreatic Polypeptide (human) | Pancreatic Polypeptide (human). Group: Biochemicals. Grades: Purified. CAS No. 75976-10-2. Pack Sizes: 200ug. US Biological Life Sciences. |  Worldwide |
| Pancreatic Polypeptide, human | Pancreatic Polypeptide, human is a C-terminally amidated 36 amino acid peptide, which acts as a neuropeptide Y ( NPY ) Y4 / Y5 receptor agonist. Uses: Scientific research. Group: Peptides. Alternative Names: Human pancreatic polypeptide. CAS No. 75976-10-2. Pack Sizes: 500 μg; 1 mg; 5 mg. Product ID: HY-P0199. | |
| Pancreatic Polypeptide, human | Pancreatic polypeptide is an agonist of neuropeptide Y (NPY) receptors that reduces forskolin-induced cAMP accumulation in L-M(TK-) cells recombinantly expressing human and rat Y4 receptors (EC50s = 87.1 and 36.3 pM, respectively). It is believed to play an important role in the function of the gastrointestinal tract. Uses: Gastrointestinal agents. Synonyms: Human pancreatic polypeptide; L-alanyl-L-prolyl-L-leucyl-L-alpha-glutamyl-L-prolyl-L-valyl-L-tyrosyl-L-prolyl-glycyl-L-alpha-aspartyl-L-asparagyl-L-alanyl-L-threonyl-L-prolyl-L-alpha-glutamyl-L-glutaminyl-L-methionyl-L-alanyl-L-glutaminyl-L-tyrosyl-L-alanyl-L-alanyl-L-alpha-aspartyl-L-leucyl-L-arginyl-L-arginyl-L-tyrosyl-L-isoleucyl-L-asparagyl-L-methionyl-L-leucyl-L-threonyl-L-arginyl-L-prolyl-L-arginyl-L-tyrosinamide; Ala-Pro-Leu-Glu-Pro-Val-Tyr-Pro-Gly-Asp-Asn-Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr-Ala-Ala-Asp-Leu-Arg-Arg-Tyr-Ile-Asn-Met-Leu-Thr-Arg-Pro-Arg-Tyr-NH2. Grade: ≥95%. CAS No. 75976-10-2. Molecular formula: C185H287N53O54S2. Mole weight: 4181.71. | |
| Pancreatic Polypeptide, rat | Pancreatic Polypeptide, rat is an agonist of NPY receptor with high affinity at NPYR4. Synonyms: Rat pancreatic polypeptide; Ala-Pro-Leu-Glu-Pro-Met-Tyr-Pro-Gly-Asp-Tyr-Ala-Thr-His-Glu-Gln-Arg-Ala-Gln-Tyr-Glu-Thr-Gln-Leu-Arg-Arg-Tyr-Ile-Asn-Thr-Leu-Thr-Arg-Pro-Arg-Tyr-NH2; L-alanyl-L-prolyl-L-leucyl-L-alpha-glutamyl-L-prolyl-L-methionyl-L-tyrosyl-L-prolyl-glycyl-L-alpha-aspartyl-L-tyrosyl-L-alanyl-L-threonyl-L-histidyl-L-alpha-glutamyl-L-glutaminyl-L-arginyl-L-alanyl-L-glutaminyl-L-tyrosyl-L-alpha-glutamyl-L-threonyl-L-glutaminyl-L-leucyl-L-arginyl-L-arginyl-L-tyrosyl-L-isoleucyl-L-asparagyl-L-threonyl-L-leucyl-L-threonyl-L-arginyl-L-prolyl-L-arginyl-L-tyrosinamide. Grade: ≥95%. CAS No. 90419-12-8. Molecular formula: C195H298N58O57S. Mole weight: 4398.87. | |
| Biotinyl-Pancreatic Polypeptide (human) | Biotinyl-Pancreatic Polypeptide (human). Synonyms: Biotin-Pancreatic Polypeptide, human; Biotinyl-Ala-Pro-Leu-Glu-Pro-Val-Tyr-Pro-Gly-Asp-Asn-Ala-Thr-Pro-Glu-Gln-Met-Ala-Gln-Tyr-Ala-Ala-Asp-Leu-Arg-Arg-Tyr-Ile-Asn-Met-Leu-Thr-Arg-Pro-Arg-Tyr-NH2. Grade: ≥95% by HPLC. CAS No. 1816258-36-2. Molecular formula: C195H301N55O56S3. Mole weight: 4408.01. | |
| Amylin (1-20), human | Amylin (1-20), human is a fragment of Amylin. Amylin, islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic β-cells. It inhibits insulin-stimulated glucose uptake, delays gastric emptying and promotes satiety. Synonyms: Lys-Leu-Gln-Lys-Ala-Asp-Ile-Glu-Glu-Ile-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-NH2 (Disulfide bond Cys2/Cys7). Molecular formula: C103H170N30O30. Mole weight: 2308.80. | |
| Amylin (20-29) (human) | Amylin (20-29) (human) forms fibrils ultrastructurally identical to amyloid fibrils seen in pancreatic islets. The region SNNFGAILSS appears to be the most important amyloidogenic sequence of hIAPP (human islet amyloid polypeptide). Synonyms: H-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-OH; L-seryl-L-asparagyl-L-asparagyl-L-phenylalanyl-glycyl-L-alanyl-L-isoleucyl-L-leucyl-L-seryl-L-serine; Amylin Fragment 20-29 human; Diabetes Associated Peptide Fragment 20-29 human; hIAPP 20-29. Grade: 95%. CAS No. 118068-30-7. Molecular formula: C43H68N12O16. Mole weight: 1009.07. | |
| Amylin (21-32), human | Amylin (21-32), human is a fragment of Amylin. Amylin, islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic β-cells. It inhibits insulin-stimulated glucose uptake, delays gastric emptying and promotes satiety. Synonyms: Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val. Molecular formula: C53H85N15O19. Mole weight: 1236.41. | |
| Amylin (22-28), human | Amylin (22-28), human is a fragment of Amylin. Amylin, islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic β-cells. It inhibits insulin-stimulated glucose uptake, delays gastric emptying and promotes satiety. Synonyms: Asn-Phe-Gly-Ala-Ile-Leu-Ser. Molecular formula: C33H52N8O10. Mole weight: 720.86. | |
| Amylin (8-18), human | Amylin (8-18), human is a fragment of Amylin. Amylin, islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic β-cells. It inhibits insulin-stimulated glucose uptake, delays gastric emptying and promotes satiety. Synonyms: Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His. Molecular formula: C57H92N18O15. Mole weight: 1269.46. | |
| Amylin, amide, human | Amylin, amide, human, a 37-amino acid polypeptide, is a pancreatic hormone cosecreted with insulin that exerts unique roles in metabolism and glucose homeostasis. Amylin, amide, human inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent[1]. Uses: Scientific research. Group: Peptides. Alternative Names: DAP amide, human. CAS No. 122384-88-7. Pack Sizes: 500 ?g; 1 mg; 5 mg. Product ID: HY-P1070. | |
| Amylin (human) | Amylin, islet Amyloid Polypeptide (IAPP), is a 37-residue peptide hormone secreted by pancreatic β-cells. It inhibits insulin-stimulated glucose uptake, delays gastric emptying and promotes satiety. It has glucose lowering effects in vivo. It is also used to study the mechanisms of amyloid deposition and its role in molecular misfolding processes expecially in conditions such as diabetes type II. Synonyms: L-Tyrosinamide, L-lysyl-L-cysteinyl-L-asparaginyl-L-threonyl-L-alanyl-L-threonyl-L-cysteinyl-L-alanyl-L-threonyl-L-glutaminyl-L-arginyl-L-leucyl-L-alanyl-L-asparaginyl-L-phenylalanyl-L-leucyl-L-valyl-L-histidyl-L-seryl-L-seryl-L-asparaginyl-L-asparaginyl-L-phenylalanylglycyl-L-alanyl-L-isoleucyl-L-leucyl-L-seryl-L-seryl-L-threonyl-L-asparaginyl-L-valylglycyl-L-seryl-L-asparaginyl-L-threonyl-, cyclic (2→7)-disulfide; AC 001; Amlintide; Amylin (human clone WO2013/156594-SEQID-1); Diabetes-associated peptide (human); Human amylin; Human IAPP; Human islet amyloid peptide; Human islet amyloid polypeptide; Human islet amyloid polypeptide-NH2; Islet amyloid polypeptide (human); H-Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr-NH2 (Disulfide bridge: Cys2-Cys7). Grade: 95%. CAS No. 122384-88-7. Molecular formula: C165H261N51O55S2. Mole weight: 3903.33. | |
| Amylin (human) (amidated) trifluoroacetate salt | Amylin is a pancreatic β-cell hormone that produces effects in several different organ systems. Amylin is a 37-amino-acid peptide that activates its specific receptors, which are multisubunit G protein and resulting in multiple receptor subtypes. Amylin's major role is as a glucoregulatory hormone, and it is an important regulator of energy metabolism in health and disease. Amidated amylin increases the rate of glycogen synthesis induced by insulin in isolated rat soleus muscle when used at a concentration of 1 nM, while linear non-amidated amylin has no effect. Synonyms: IAPP (human) (amidated); Islet Amyloid Polypeptide (human) (amidated). Grade: ≥95%. Molecular formula: C165H261N51O55S2·xCF3COOH. Mole weight: 3903.28. | |
| Amylin (human) trifluoroacetate salt | Amylin is a pancreatic β-cell hormone that produces effects in several different organ systems. Amylin is a 37-amino-acid peptide that activates its specific receptors, which are multisubunit G protein and resulting in multiple receptor subtypes. Amylin's major role is as a glucoregulatory hormone, and it is an important regulator of energy metabolism in health and disease. Amidated amylin increases the rate of glycogen synthesis induced by insulin in isolated rat soleus muscle when used at a concentration of 1 nM, while linear non-amidated amylin has no effect. Synonyms: IAPP (human); Islet Amyloid Polypeptide (human). Grade: ≥95%. Molecular formula: C165H260N50O56S2·xCF3COOH. Mole weight: 3904.27. | |
| Amylin (rat) | Amylin (rat), islet Amyloid Polypeptide (IAPP), is a glucoregulatory peptide from rat pancreatic cells. It inhibits glucagon secretion, delays gastric emptying and acts as a satiety agent. It is used to study the regulation of satiety and obesity. It binds to heteromeric complexes of human calcitonin receptor 2 (CTR2) with receptor activity-modifying protein (RAMP) 1 or 3. It also binds to mouse α-thyroid-stimulating hormone thyrotroph (α-TSH) cells and rat nucleus accumbens membrane preparations. It inhibits insulin-induced, but not basal, glycogen synthesis in hepatocytes isolated from fasted rats in vitro. It does not form fibrils and is not cytotoxic unlike human amylin. It is active in vivo. Synonyms: Amylin, amide, rat; Amylin (mouse, rat); IAPP (mouse, rat); Islet amyloid polypeptide (mouse, rat); H-Lys-Cys(1)-Asn-Thr-Ala-Thr-Cys(1)-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-Arg-Ser-Ser-Asn-Asn-Leu-Gly-Pro-Val-Leu-Pro-Pro-Thr-Asn-Val-Gly-Ser-Asn-Thr-Tyr-NH2; L-lysyl-L-cysteinyl-L-asparagyl-L-threonyl-L-alanyl-L-threonyl-L-cysteinyl-L-alanyl-L-threonyl-L-glutaminyl-L-arginyl-L-leucyl-L-alanyl-L-a. Grade: ≥98%. CAS No. 124447-81-0. Molecular formula: C167H272N52O53S2. Mole weight: 3920.43. | |
| Amylin (rat, mouse) trifluoroacetate salt | Amylin is a pancreatic β-cell hormone that produces effects in several different organ systems. Amylin is a 37-amino-acid peptide that activates its specific receptors, which are multisubunit G protein and resulting in multiple receptor subtypes. Amylin's major role is as a glucoregulatory hormone, and it is an important regulator of energy metabolism in health and disease. Amidated amylin increases the rate of glycogen synthesis induced by insulin in isolated rat soleus muscle when used at a concentration of 1 nM, while linear non-amidated amylin has no effect. Synonyms: IAPP (rat, mouse); Islet Amyloid Polypeptide (rat, mouse). Grade: ≥95%. Molecular formula: C167H272N52O53S2·xCF3COOH. Mole weight: 3920.40. | |
| Aprotinin | Aprotinin is the small protein bovine pancreatic trypsin inhibitor (BPTI). It is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. It is a competitive serine protease inhibitor which blocks the active sites of enzyme by forming stable complexes with. It is a monomeric globular protein derived from bovine lung that consists of 58 amino acids, arranged in a single polypeptide chain with three crosslinking disulfide bridges. It is used as a medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. It is used clinically to prevent postoperative blood loss and reduce transfusion requirements in those procedures which employ extracorporeal circulation. It is also used as a protein purification tool to prevent proteases present in tissue samples from degrading the protein of interest. It was temporarily withdrawn worldwide in 2007. It was reverted its previous standpoint regarding aprotinin by the European Medicines Agency (EMA) scientific committee in February 2012. Uses: Aprotinin is used as medication administered by injection to reduce bleeding during complex surgery, such as heart and liver surgery. it is used clinically to prevent postoperative blood loss and reduce transfusion requirements in those procedures which employ extracorporeal circulation. it is also used as a protein purification tool to prevent proteases present in tissue sample | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C |  |
| Carboxypeptidase-B rat, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit...sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| GIP (1-39) | GIP (1-39) is an endogenous truncated form of the incretin hormone GIP. GIP (1-39) has the high potency at stimulating glucose-dependent insulin secretion from rat pancreatic β-cells than GIP. Synonyms: Gastric Inhibitory Polypeptide (1-39). CAS No. 725474-97-5. Molecular formula: C210H316N56O61S. Mole weight: 4633.21. | |
| GIP (human) | GIP (human) is a potent insulinotropic hormone synthesized by duodenal K-cells. It inhibits gastric acid secretion and stimulates pancreatic insulin release in response to glucose. Synonyms: Gastric Inhibitory Polypeptide human; Gastric Inhibitory Polypeptide (human); Gastric Inhibitory Peptide (GIP), human; Tyr-Ala-Glu-Gly-Thr-Phe-Ile-Ser-Asp-Tyr-Ser-Ile-Ala-Met-Asp-Lys-Ile-His-Gln-Gln-Asp-Phe-Val-Asn-Trp-Leu-Leu-Ala-Gln-Lys-Gly-Lys-Lys-Asn-Asp-Trp-Lys-His-Asn-Ile-Thr-Gln. Grade: 95%. CAS No. 100040-31-1. Molecular formula: C226H338N60O66S. Mole weight: 4983.58. | |
| GIP (mouse) | GIP (mouse) is a gastrointestinal hormone that is expressed in and secreted from the pancreatic islets and promotes insulin secretion [1]. Uses: Scientific research. Group: Peptides. Alternative Names: Gastric inhibitory polypeptide(mouse); GIP(1-42) (mouse). CAS No. 181591-59-3. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-P10735. | |
| GRPP (human) | GRPP (human) is a synthetic analogue of a cleavage product resulting from proglucagon processing in pancreatic α- and intestinal L-cells. Synonyms: Preproglucagon (21-50) (human); H-Arg-Ser-Leu-Gln-Asp-Thr-Glu-Glu-Lys-Ser-Arg-Ser-Phe-Ser-Ala-Ser-Gln-Ala-Asp-Pro-Leu-Ser-Asp-Pro-Asp-Gln-Met-Asn-Glu-Asp-OH; glicentin-related polypeptide (human); L-arginyl-L-seryl-L-leucyl-L-glutaminyl-L-alpha-aspartyl-L-threonyl-L-alpha-glutamyl-L-alpha-glutamyl-L-lysyl-L-seryl-L-arginyl-L-seryl-L-phenylalanyl-L-seryl-L-alanyl-L-seryl-L-glutaminyl-L-alanyl-L-alpha-aspartyl-L-prolyl-L-leucyl-L-seryl-L-alpha-aspartyl-L-prolyl-L-alpha-aspartyl-L-glutaminyl-L-methionyl-L-asparagyl-L-alpha-glutamyl-L-aspartic acid. Grade: ≥95%. CAS No. 1132745-52-8. Molecular formula: C136H215N41O58S. Mole weight: 3384.47. | |
| Insulin (cattle) | Insulin (cattle) is a polypeptide hormone that regulates glucose metabolism in pancreatic islet B cells. Synonyms: Insulin from bovine pancreas; Phe-Val-Asn-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala. Gly-Ile-Val-Glu-Gln-Cys-Cys-Ala-Ser-Val-Cys-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys-Asn (Disulfide bridge: Cys7-Cys7', Cys19-Cys20', Cys6'-Cys11'). Grade: ≥97%. CAS No. 11070-73-8. Molecular formula: C254H377N65O75S6. Mole weight: 5733.49. | |
| Insulin(cattle) | Insulin cattle is a two-chain polypeptide hormone produced in vivo in the pancreatic β cells. Insulin cattle has often been used as growth supplement in culturing cells. Uses: Scientific research. Group: Peptides. CAS No. 11070-73-8. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P1156. | |
| Insulin (human) | Two-chain polypeptide hormone produced by the β-cells of pancreatic islets. Its molecular weight is ~5800 Da. The α and β chains are joined by two interchain disulfide bonds. The α chain contains an intrachain disulfide bond. Insulin regulates the cellular uptake, utilization, and storage of glucose, amino acids, and fatty acids and inhibits the breakdown of glycogen, protein, and fat. Synonyms: Recombinant human insulin; Insulin human; H-Phe-Val-Asn-Gln-His-Leu-Cys(1)-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Tyr-Leu-Val-Cys(2)-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Thr-OH.H-Gly-Ile-Val-Glu-Gln-Cys(3)-Cys(1)-Thr-Ser-Ile-Cys(3)-Ser-Leu-Tyr-Gln-Leu-Glu-Asn-Tyr-Cys(2)-Asn-OH; L-phenylalanyl-L-valyl-L-asparagyl-L-glutaminyl-L-histidyl-L-leucyl-L-cysteinyl-glycyl-L-seryl-L-histidyl-L-leucyl-L-valyl-L-alpha-glutamyl-L-alanyl-L-leucyl-L-tyrosyl-L-leucyl-L-valyl-L-cysteinyl-glycyl-L-alpha-glutamyl-L-arginyl-glycyl-L-phenylalanyl-L-phenylalanyl-L-tyrosyl-L-threonyl-L-prolyl-L-lysyl-L-threonine (7->7'),(19->20')-bis(disulfide) compound with glycyl-L-isoleucyl-L-valyl-L-alpha-glutamyl-L-glutaminyl-L-cysteinyl-L-cysteinyl-L-threonyl-L-seryl-L-isoleucyl-L-cysteinyl-L-seryl-L-leucyl-L-tyrosyl-L-glutaminyl-L-leucyl-L-alpha-glutamyl-L-asparagyl-L-tyrosyl-L-cysteinyl-L-asparagine (6'->11')-disulfide. Grade: 95%. CAS No. 11061-68-0. Molecular formula: C257H383N65O77S6. Mole weight: 5807.57. | |
| [Leu31,Pro34]-Neuropeptide Y (porcine) | [Leu31,Pro34]-Neuropeptide Y (porcine) is a high affinity neuropeptide Y Y1 receptor agonist (Ki = 0.54 nM). Synonyms: (Leu(31),pro(34))npy; 31-Leu-34-pro-neuropeptide Y; Pancreatic polypeptide (chicken), 1-L-tyrosine-4-L-lysine-6-L-aspartic acid-7-L-asparagine-10-L-glutamic acid-14-L-alanine-18-L-alanine-20-L-tyrosine-22-L-serine-23-L-alanine-25-L-arginine-26-L-histidine-28-L-isoleucine-30-L-leucine-31-L-leucine-34-L-proline. CAS No. 125580-28-1. Molecular formula: C190H286N54O56. Mole weight: 4222.63. | |
| Native Bovine α-Chymotrypsin | Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Chymotrypsin (ec 3.4.21.1, chymotrypsins a and b, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chym...ate p1 sidechain and the enzyme s1 binding cavity accounts for the substrate specificity of this enzyme. chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the p1 position. structurally, it is the archetypal structure for its superfamily, the pa clan of proteases. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Activity: > 40 units/mg protein. Sto | |
| Native Human α-Chymotrypsin | Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chy. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Mole weight: mol wt 25 kDa. Storage: -20°C. Form: lyophilized powder. Source: Human pancreas. Species: Human. EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Cat No: NATE-0747. | |
| Native Human Carboxypeptidase B | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Applications: Carboxypeptidase b from creative enzymes has been used as a reference for assaying carboxypeptidase ...ino acids, to get a distinct band for each allotype during c4 electrophoresis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Solution in 0.05 M NaOAc pH 5.0 + 1.0 M NaCl + 0.01% NaN3. Source: Human pancreas. Species: Human. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0151. | |
| Native Porcine Carboxypeptidase B | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Protein determined by biuret. Applications: Carboxypeptidase b has been used in a study to develop a non-invasive...ith carboxypeptidase b, which is a c-terminal lysine-specific endopeptidase, is measured using flow cytometry analysis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Storage: -20°C. Form: lyophilized powder. Contains HEPES buffer salts and carbohydrate. Source: Porcine pancreas. Species: Porcine. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0152. | |
| RNase B, Bovine Pancreas | RNase B, Bovine Pancreas is an N-glycosylated form of bovine pancreatic ribonuclease, which is structurally analogous to RNase A. RNase B, Bovine Pancreas promotes the folding of polypeptide chains and performs a chaperone-like function[1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Ribonuclease B, Bovine Pancreas. Pack Sizes: 25 mg; 50 mg; 100 mg. Product ID: HY-129046C. | |
| (S)-VU0637120 | (S)-VU0637120 is a selective antagonist of neuropeptide Y4 receptor, which belongs to the superfamily of G protein-coupled receptors and plays an important role in the regulation of food intake and energy metabolism. (S)-VU0637120 selectively inhibits native Y4R function and binds in an allosteric site located below the binding pocket of the endogenous ligand pancreatic polypeptide in the core of the Y4R transmembrane domains. Synonyms: (2S)-N-(6,7-Dihydro[1,4]dioxino[2,3-f]benzothiazol-2-yl)-1-(methylsulfonyl)-2-piperidinecarboxamide. Grade: 99%. CAS No. 1175940-86-9. Molecular formula: C16H19N3O5S2. Mole weight: 397.47. | |
| Elastase, Porcine pancreas | Elastase, Porcine pancreas (EC 3.4.21.36) is a single polypeptide chain of 240 amino acid residues, derived from pig pancreas. Elastase, Porcine pancreas is a serine protease that can hydrolyze proteins and polypeptide. Elastase from porcine pancreas can induce emphysema in hamsters [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 3.4.21.36; Pancreatopeptidase E. CAS No. 39445-21-1. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P2974. | |
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