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Supplier: Ambeed
Description: L-Tyrosine amide 98%

Catalog Number: (E-2520.0005BA)
Supplier: Bachem Americas
Description: Sequence: H-Tyr-NH₂


Supplier: Promega Corporation
Description: Recombinant full-length human LYN B was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. LYN is a 56kDa tyrosine kinase that is similar to mouse T-lymphocyte-specific tyrosine kinase p56lck, v-yes, v-fgr and v-src.
Supplier: Bachem Americas
Description: Ac-IYGEF-amide, excellent small peptide substrate for the protein tyrosine kinase pp60c-src (Km= 368 µM and Vmax= 1.02 µmol min⁻¹ mg⁻¹).

Catalog Number: (PAV9501)
Supplier: Promega Corporation
Description: Recombinant full-length human LYN B was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag. LYN is a 56kDa tyrosine kinase that is similar to mouse T-lymphocyte-specific tyrosine kinase p56lck, v-yes, v-fgr and v-src.


Catalog Number: (95053-370)
Supplier: Enzo Life Sciences
Description: Peptide tyrosine-tyrosine (PYY) amide is a 36 amino-acid. PYY is a member of the pancreatic polypeptide (PP) family of peptides (neuropeptide Y (NPY), PYY and PP). While NPY is localized in neurons (both in the central and peripheral nervous system) and PP in the pancreatic islets, PYY is found in both neurons and the gut. PYY is released in response to food intake from the same endocrine cells (L cells) in the intestinal mucosa as the glucagon-like peptides, and inhibits gall bladder secretion, gut motility and pancreatic secretion. These effects are similar to those of PP and overlap with the gut inhibitory activity of GLP-1.


Catalog Number: (PAV9741)
Supplier: Promega Corporation
Description: Recombinant full-length human SRC was expressed in E. coli cells using an N-terminal GST tag. SRC was originally identified as a transforming protein of the Rous sarcoma virus that had enzymatic ability to phosphorylate tyrosine in protein substrates.


Catalog Number: (77440-472)
Supplier: Bioss
Description: This gene encodes a protein with 13 putative coiled-coil domains, a region with homology to SMC chromosome segregation ATPases, six KID motifs, three tropomyosin homology domains and an ATP/GTP binding site motif A. The protein is localized to the centrosome and cilia and has sites for N-glycosylation, tyrosine sulfation, phosphorylation, N-myristoylation, and amidation. Mutations in this gene have been associated with Joubert syndrome and nephronophthisis and the presence of antibodies against this protein is associated with several forms of cancer. (provided by RefSeq, Jul 2008.

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Catalog Number: (100294-986)
Supplier: Indofine Chemical Company
Description: Rare Organics & BioChemicals 1989-39-6 5gm Z-Tyr-NH2 314.4 Room temperature.

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Catalog Number: (102996-112)
Supplier: Anaspec Inc
Description: Like human Gastrin-1 “Little Gastrin,” rat Gastrin-1 “Little Gastrin” contains 17 amino acids, but differs from human Gastrin by 3 amino acids at the C-terminus. Secretion of Gastrin is induced by food intake and causes the release of gastric acid. Synthesized by the G cells in the gastric mucosa, it is one of the major bioactive forms of Gastrin (the other bioactive form is Gastrin-34). Both Gastrin-17 and Gastrin-34 are carboxy-amidated and partially tyrosine sulfated. Binding of Gastrin to the CCK2/gastrin receptor requires carboxy-amidation, however sulfation is not necessary for binding to the receptor.
Sequence: Pyr-RPPMEEEEEAYGWMDF-NH2
MW: 2126.3 Da
% Peak area by HPLC: 95
Storage condition: -20° C


Catalog Number: (10285-120)
Supplier: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.


Catalog Number: (10285-108)
Supplier: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.


Catalog Number: (10288-472)
Supplier: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.


Catalog Number: (102996-108)
Supplier: Anaspec Inc
Description: Big Gastrin is also referred to as Gastrin-34. Secretion of gastrin is induced by food intake and causes the release of gastric acid in the stomach. Secreted by the G cells in the gastric mucosa, it is one of the major bioactive forms of gastrin found in tissue and plasma (the other bioactive form is gastrin-17 or little gastrin - Cat# AS-20750). Both gastrin-17 and gastrin-34 are carboxy-amidated and partially tyrosine sulfated. Binding of gastrin to the CCK2/gastrin receptor requires carboxy-amidation, however sulfation is not necessary for binding to the receptor. Binding of Gastrin to the CCK2/gastrin receptors on parietal cells of the stomach causes them to secrete hydrochloric acid (HCl) and stimulates lectin-like protein Reg expression via activation of PKC and RhoA. Gastrin also plays a role in release of Histamine and Pepsinogen.
Sequence: Pyr-LGPQGPPHLVADPSKKQGPWLEEEEEAYGWMDF-NH2
MW: 3849.3 Da
% Peak area by HPLC: 95
Storage condition: -20° C


Catalog Number: (102996-110)
Supplier: Anaspec Inc
Description: Gastrin-1 is also referred to as Gastrin-17 or “Little Gastrin.” Secretion of gastrin is induced by food intake and causes the release of gastric acid in the stomach. Secreted by the G cells in the gastric mucosa, it is one of the major bioactive forms of gastrin found in tissue and plasma (the other bioactive form is Gastrin-34 or Big Gastrin - Cat# AS-20747). Both Gastrin-17 and Gastrin-34 are carboxy-amidated and partially tyrosine sulfated. Binding of Gastrin to the CCK2/gastrin receptor requires carboxy-amidation, however sulfation is not necessary for binding to the receptor. Binding of Gastrin to the CCK2/Gastrin receptors on parietal cells of the stomach causes them to secrete hydrochloric acid (HCl) and stimulates lectin-like protein Reg expression via activation of PKC and RhoA. Gastrin also plays a role in release of Histamine and Pepsinogen.
Sequence: Pyr-GPWLEEEEEAYGWMDF-NH2
MW: 2098.2 Da
% Peak area by HPLC: 95
Storage condition: -20° C


Catalog Number: (10288-466)
Supplier: Bioss
Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.


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