ENSA Protein

ArtNr	OPPA02085
Hersteller	AVIVA Systems Biology
Menge	5 ug
Kategorie	Peptides & Proteins Recombinant Proteins
Typ	Proteins Recombinant
Format	Liquid
Specific against	Human (Homo sapiens)
Host	E.coli
Purity	Greater than 90.0% as determined by SDS-PAGE.
Sequence	MGSSHHHHHH SSGLVPRGSH MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E.
ECLASS 10.1	32160409
ECLASS 11.0	32160409
UNSPSC	12352202
Alias	ARPP-19e
Similar products	ENSA
Versandbedingung	Gekühlt
Lieferbar
Manufacturer - Type	Protein
Manufacturer - Category	Root Catalog/Products/Recombinant Proteins
Shipping Temperature	Wet Ice
Gene symbol	ENSA
Protein size	Recombinant
Product format	The Endosulfine Alpha protein solution contains 20mM Tris, pH-8, 1mM DTT and 10% glycerol. Physical appearance: Sterile filtered colorless solution.
Reconstitution and storage	Store at 4C if entire vial will be used within 2-4 weeks. Store, frozen at -20C for longer periods of time. For long term storage it is recommended to add a carrier protein (0. 1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Description of target	ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.
Protein accession_num	NP_004427.1
Protein name	Alpha-endosulfine
Purification	The ENSA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

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OPPA02085-datasheet.pdf

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Menge: 5 ug

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Lieferung vsl. bis 13.11.2025

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