VAMP3 Human

Synaptobrevin-3 Human Recombinant
Cat. No.
BT5654
Source
Escherichia Coli.
Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis 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

VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

Product Specs

Introduction
VAMP3, also known as cellubrevin, is a protein found in recycling endosomes and their vesicles. It plays a crucial role in various cellular processes, including the recycling of transferrin receptors to the plasma membrane, the secretion of alpha-granules in platelets, the recycling of T-cell receptors to immunological synapses, and membrane trafficking during cell migration. In platelets, VAMP3 is essential for granule secretion. As a member of the synaptobrevin family, VAMP3 is a key component of the protein complex responsible for the docking and/or fusion of synaptic vesicles with the presynaptic membrane. Its widespread tissue distribution and subcellular localization, along with its high homology to other VAMPs, indicate that it is the human counterpart of rodent cellubrevin. Notably, in platelets, VAMP3 resides in a compartment that remains immobile from the plasma membrane even upon calcium or thrombin stimulation.
Description
Recombinant human VAMP3, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 8.7 kDa, comprising 77 amino acids.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The VAMP3 protein solution is provided in 20mM Tris buffer at pH 7.5 with 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, adding a carrier protein (0.1% HSA or BSA) is advised. It is crucial to avoid repeated freeze-thaw cycles.
Purity
The purity of VAMP3 is greater than 95.0%, as determined by Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis.
Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Source
Escherichia Coli.
Amino Acid Sequence
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

Product Science Overview

Introduction

Synaptobrevin-3, also known as Vesicle-Associated Membrane Protein 3 (VAMP3), is a member of the SNARE (Soluble NSF Attachment Protein Receptor) protein family. These proteins are essential for the fusion of vesicles with target membranes, a critical process in cellular transport and communication. Synaptobrevin-3 is particularly important in the context of synaptic vesicle exocytosis, where it plays a key role in neurotransmitter release.

Structure and Function

Synaptobrevin-3 is an integral membrane protein with a molecular weight of approximately 18 kilodaltons (kDa). It is characterized by a single transmembrane domain, a cytoplasmic domain that participates in SNARE complex formation, and a short luminal domain. The SNARE complex is composed of four α-helices: one contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 .

The primary function of Synaptobrevin-3 is to mediate the fusion of synaptic vesicles with the presynaptic membrane, facilitating the release of neurotransmitters into the synaptic cleft. This process is tightly regulated by calcium ions and involves the formation of a highly stable SNARE complex .

Synaptobrevin-3 in Human Health

Synaptobrevin-3 is crucial for normal neuronal function. Disruptions in its activity can lead to severe neurological disorders. For instance, the botulinum toxin, produced by the bacterium Clostridium botulinum, targets and cleaves synaptobrevin, leading to paralysis by preventing neurotransmitter release .

Recombinant Synaptobrevin-3

Recombinant Synaptobrevin-3 is produced using genetic engineering techniques, where the gene encoding Synaptobrevin-3 is inserted into an expression system, typically bacterial or mammalian cells, to produce the protein in large quantities. This recombinant protein is used in various research applications, including studies on vesicle fusion, neurotransmitter release, and the development of therapeutic agents targeting SNARE proteins.

Research and Clinical Applications

Research on Synaptobrevin-3 has provided significant insights into the mechanisms of synaptic transmission and the role of SNARE proteins in cellular communication. Understanding the function and regulation of Synaptobrevin-3 can lead to the development of novel therapeutic strategies for treating neurological disorders such as epilepsy, depression, and neurodegenerative diseases .

In clinical settings, recombinant Synaptobrevin-3 can be used to study the effects of toxins, such as botulinum toxin, and to develop inhibitors that can modulate SNARE complex formation and function. This has potential applications in treating conditions caused by excessive neurotransmitter release, such as spasticity and certain types of chronic pain .

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