AnaSpec News

Eleven New Peptides - July 19, 2007

This week AnaSpec introduced eleven (11) new peptides for drug discovery research.

MUC5AC; Analog 1 - Cat# 61329, 1 mg
This peptide is derived from the human mucin MUC5AC gene sequence. Data suggest that MUC5A and MUC5C are part of the same gene MUC5AC; which is distinct from MUC5B. The gene MUC5AC is mainly expressed in gastric; tracheo-bronchial mucosae and some tumors; it exhibits two kinds of deduced peptide domains; one of which is 8 amino acid tandemly repeated domain; a consensus peptide TTSTTSAP.
Sequence: GTTPSPVPTTSTTSAP

[Ile12; Val15] MUC5AC Analog 3 - Cat# 61331, 1 mg
This sequence corresponds to the sequence found naturally in mucin-type MUC5AC glycoprotein; but with 2 amino acid substitutions - a reflection of mucin molecule polymorphism. MUC5AC gene is mainly expressed in gastric and tracheo-bronchial mucosae.
Sequence: GTTPSPVPTTSITSVP

[Ala6; Val15] MUC5AC Analog 2 - Cat# 61330, 1 mg
This is a mucin peptide MUC5AC motif with 2 amino acid substitutions that are a reflection of mucin molecule polymorphism. Mucin-type O-glycosylation is regulated by a repertoire of ppGaNTase enzymes; the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family. A panel of modified peptides; including this peptide; is used to detect ppGaNTase activity in vitro.
Sequence: GTTPSAVPTTSTTSVP

MUC5AC-3/13 - Cat# 61332, 1 mg
This is a MUC5AC peptide with two sites (Thr3 and Thr13) labeled with GalNAc where the asterisk denotes GalNAc-modified residues. Mucin type O-linked glycosylation is initiated by the action of a family of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferases (ppGaNTase); which catalyze the transfer of GalNAc from the nucleotide sugar UDP-GalNAc to the hydroxyl group of either serine or threonine.
Sequence: GT-T*-PSPVPTTST-T*-SAP

MUC5AC; Analog B - Cat# 61335, 1 mg
This peptide is a fragment of human mucin 5 containing consensus peptide TTSTTSAP repeated domains. MUC5AC represents a mucin peptide core expressed in normal gastric epithelia and some tumors.
Sequence: TTSTTSAPTTS

MUC5AC 3 - Cat# 61334, 1 mg
This peptide is a 16 amino acid modified fragment of mucin 5/MUC5AC; where T* is a GalNac labeled threonine 3. Mucin-type linkages (GalNAc 1-O-Ser/Thr) are initiated by a family of glycosyltransferases known as the UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGaNTases). These enzymes transfer GalNAc from the sugar donor UDP-GalNAc to serine and threonine residues; forming an alpha anomeric linkage. The MUC5AC gene; which is mainly expressed in gastric and respiratory mucosae; exhibits 8 amino acid tandemly repeated domain; the consensus peptide TTSTTSAP.
Sequence: GT-T*-PSPVPTTSTTSAP

Aquaporin-2 (255-271); human - Cat# 61326, 1 mg
This is a fragment of human aquaporin-2 (AQP2); amino acids 255 to 271. AQP2 is one of the water-channel proteins expressed in principal cells of kidney collecting ducts; where it is stored in the intracellular compartment.
Sequence: QSVELHSPQSLPRGSKA

Aquaporin-2 (255-271); rat - Cat# 61327, 1 mg
This is a fragment of rat aquaporin-2 (AQP2). Aquaporins are water channels. They form pores in the membranes of cells and selectively pass water molecules through the membrane.
Sequence: QSVELHSPQSLPRGTKA

Aquaporin-2 (254-267); pSER261; human - Cat# 61328, 1 mg
This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser261. Protein phosphorylation plays a key role in vasopressin signaling in renal-collecting duct. Phosphorylation at several AQP2 residues including Ser256 and Ser261; is altered in response to vasopressin. It is possible that both sites are involved in vasopressin-dependent AQP2 trafficking. Sequence: RQSVELH-pS-PQSLPR

Aquaporin-2 (254-267); pSER256; human - Cat# 61325, 1 mg
This peptide is a fragment of the human aquaporin-2 (AQP2) phosphorylated at Ser256. Protein phosphorylation plays a key role in vasopressin signaling in the renal-collecting duct. AQP2 residues including S256 and S261; are altered in response to vasopressin. In the presence of vasopressin; AQP2 monophosphorylated at Ser256 and diphosphorylated AQP2 (pSer256/261) increase in abundance; whereas AQP2 monophosphorylated at Ser261 decreases; suggesting that both sites are involved in vasopressin-dependent AQP2 trafficking. Aquaporins are water channels. They form pores in the membranes of cells and selectively pass water molecules through the membrane; and prevent the crossing of sodium; potassium and other ions and small molecules.
Sequence: RQ-pS-VELHSPQSLPR

Aquaporin-2 (254-267); human - Cat# 61324, 1 mg
This peptide is a fragment of the human aquaporin-2 (AQP2) which is primarily expressed in renal collecting ducts and is altered in response to vasopressin via phosphorylation of several phosphorylation sites. Aquaporins are water channels. They form pores in the membranes of cells and selectively pass water molecules through the membrane; and prevent the crossing of sodium; potassium and other ions and small molecules.
Sequence: RQSVELHSPQSLPR

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