VAMP7 Human

Vesicle-Associated Membrane Protein 7 Human Recombinant
Cat. No.
BT5912
Source
E.coli.
Synonyms
Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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.
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Description

VAMP7 Human Recombinant produced in E. coli is a single polypeptide chain containing 211 amino acids (1-188) and having a molecular mass of 23.0 kDa.
VAMP7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
VAMP7 (Vesicle-Associated Membrane Protein 7), a member of the synaptobrevin family, is a transmembrane protein belonging to the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. This protein plays a crucial role in the intracellular transport system, specifically in targeting and fusing transport vesicles with their destination membranes. VAMP7 is primarily involved in transporting proteins from the early endosome to the lysosome. Its localization in late endosomes and lysosomes is vital for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. VAMP7 is also essential for calcium-regulated lysosomal exocytosis, the export of chylomicrons from the endoplasmic reticulum to the cis Golgi, and exocytosis of mediators during eosinophil and neutrophil degranulation. Furthermore, VAMP7 is necessary for target cell killing by natural killer cells.
Description
Recombinant human VAMP7, expressed in E. coli, is a single polypeptide chain. This protein consists of 211 amino acids, with a sequence encompassing residues 1-188 of the native protein, and has a molecular weight of 23.0 kDa. For purification purposes, a 23 amino acid His-tag is fused to the N-terminus of the protein. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
VAMP7 is supplied in a solution format at a concentration of 0.5mg/ml. The solution is buffered with 20mM Tris-HCl at pH 8.0 and also contains 0.15M NaCl and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), the VAMP7 solution should be stored at 4°C. For long-term storage, it is recommended to store the solution at -20°C. To ensure stability during long-term storage, the addition of a carrier protein like HSA or BSA to a final concentration of 0.1% is advisable. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of VAMP7 is determined by SDS-PAGE analysis and is guaranteed to be greater than 90%.
Synonyms
Vesicle-associated membrane protein 7, Tetanus-insensitive VAMP, tetanus neurotoxin-insensitive VAMP, Synaptobrevin-like protein 1, TI-VAMP, VAMP-7, TIVAMP, SYBL1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAILFAV VARGTTILAK HAWCGGNFLE VTEQILAKIP SENNKLTYSH GNYLFHYICQ DRIVYLCITD DDFERSRAFN FLNEIKKRFQ TTYGSRAQTA LPYAMNSEFS SVLAAQLKHH SENKGLDKVM ETQAQVDELK GIMVRNIDLV AQRGERLELL IDKTENLVDS SVTFKTTSRN LARAMCMKNL K

Product Science Overview

Introduction

Vesicle-Associated Membrane Protein 7 (VAMP7), also known as SYBL1 or TI-VAMP, is a transmembrane protein that plays a crucial role in the intracellular transport system. It is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family, which is essential for the fusion of vesicles with their target membranes .

Gene and Protein Structure

The VAMP7 gene is located on the X chromosome (Xq28) and encodes a protein that is approximately 220 amino acids long . The protein structure includes a longin domain, a SNARE motif, and a transmembrane domain. The longin domain is involved in the regulation of the protein’s function, while the SNARE motif is critical for the fusion of vesicles with target membranes .

Function

VAMP7 is primarily involved in the targeting and fusion of transport vesicles to their target membranes. It localizes to late endosomes and lysosomes and is essential for the heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion . Additionally, VAMP7 is required for calcium-regulated lysosomal exocytosis, which is crucial for various cellular processes, including the release of enzymes and other molecules from lysosomes .

Biological Processes

VAMP7 plays a significant role in several biological processes, including:

  • Vesicle-Mediated Transport: It is involved in the transport of proteins from the early endosome to the lysosome .
  • Neurite Outgrowth: VAMP7 is implicated in the modulation of neurite outgrowth by regulating the transport of L1CAM to the plasma membrane .
  • Exocytosis: It is essential for the exocytosis of lysosomal contents in response to calcium signals .
Clinical Significance

Mutations or dysregulation of VAMP7 can lead to various cellular dysfunctions. Given its role in vesicle transport and exocytosis, abnormalities in VAMP7 function can impact processes such as neurotransmitter release, immune responses, and cellular waste management. Research is ongoing to understand the full spectrum of VAMP7’s involvement in human health and disease .

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