VAMP5 Human

Vesicle-associated membrane protein 5 Human Recombinant
Cat. No.
BT5806
Source
Escherichia Coli.
Synonyms
VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

VAMP5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 109 amino acids (1-72 a.a.) and having a molecular mass of 12.7 kDa.
VAMP5 is fused to 37 amino acids His Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
VAMP5, a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily, plays a role in vesicle trafficking events associated with myogenesis.
Description
Produced in E. coli, VAMP5 is a single, non-glycosylated polypeptide chain comprising 109 amino acids (amino acids 1-72) with a molecular mass of 12.7 kDa. It features a 37 amino acid His Tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The VAMP5 protein solution (0.5 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 5 mM DTT, 0.5 mM EDTA, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is advised. Avoid repeated freeze-thaw cycles.
Purity
The purity of VAMP5 is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
VAMP5, Vesicle-associated membrane protein 5, VAMP-5, Myobrevin, HSPC191.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAG IELERCQQQA NEVTEIMRNN FGKVLERGVK LAELQQRSDQ LLDMSSTFNK TTQNLAQKKC WENIRYRIC.

Product Science Overview

Introduction

Vesicle-associated membrane protein 5 (VAMP5), also known as myobrevin, is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. These proteins play a crucial role in the docking and fusion of vesicles with cell membranes, which is essential for various cellular processes, including neurotransmitter release and hormone secretion .

Gene and Protein Structure

The VAMP5 gene is located on chromosome 2 at the p11.2 locus. It encodes a protein that is involved in vesicle trafficking events associated with myogenesis, such as myoblast fusion and GLUT4 trafficking . The protein consists of a single transmembrane domain, a cytoplasmic domain, and a vesicle-associated domain, which are characteristic features of the VAMP family .

Function

VAMP5 is primarily involved in the trafficking of vesicles within cells. It is a key component of the SNARE complex, which mediates the fusion of vesicles with target membranes. This process is vital for the proper functioning of various cellular activities, including the release of neurotransmitters at synapses and the secretion of hormones .

In the context of myogenesis, VAMP5 plays a significant role in the fusion of myoblasts to form multinucleated muscle fibers. This is a critical step in muscle development and regeneration. Additionally, VAMP5 is involved in the trafficking of GLUT4, a glucose transporter, to the plasma membrane in response to insulin signaling .

Clinical Significance

Mutations or dysregulation of the VAMP5 gene have been associated with various diseases. For instance, VAMP5 has been linked to infant botulism and nephronophthisis 2 . Understanding the role of VAMP5 in these conditions can provide insights into potential therapeutic targets for treating these diseases.

Research and Applications

Recombinant VAMP5 protein is widely used in research to study vesicle trafficking and membrane fusion processes. It is also utilized in the development of assays and diagnostic tools for investigating diseases associated with vesicle trafficking defects .

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