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VAMP2 Mouse

目录号 : GP24972

Synaptobrevin-2 Recombinant Mouse

VAMP2 Mouse Chemical Structure

规格 价格 库存 购买数量
1μg
¥840.00
5-10工作日
5μg
¥2,030.00
5-10工作日
50μg
¥16,800.00
5-10工作日

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Sample solution is provided at 25 µL, 10mM.

产品文档

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产品描述

VAMP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-94 a.a) and having a molecular mass of 12.8kDa. VAMP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Data

Purity Greater than 90.0% as determined by SDS-PAGE. Source Escherichia Coli.
Phycical Appearance Sterile Filtered clear solution. Shipping Condition Shipped with Ice Packs.
Synonyms Vesicle-associated membrane protein 2; VAMP-2; Synaptobrevin-2; Vamp2; Syb2.
Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MGSHMSATAA TVPPAAPAGE GGPPAPPPNL TSNRRLQQTQ AQVDEVVDIM RVNVDKVLER DQKLSELDDR ADALQAGASQ FETSAAKLKR KYWWKNLK.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C 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.
Formulation VAMP2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM EDTA, 0.1mM PMSF and 10% glycerol.

Introduction

Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

Stability

Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C 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.