VAMP8 Human

Endobrevin Human Recombinant
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Cat. No.
BT6007
Source
Escherichia Coli.
Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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.
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Description

Molecular Structure and Function

Gene and Protein Characteristics

  • Gene Location: VAMP8 is located on chromosome 2 (2p12) in humans .

  • Protein Structure: VAMP8 is a 100-amino-acid protein with a conserved SNARE motif (residues 29–93) essential for forming trans-SNARE complexes .

  • Interactions: VAMP8 interacts with syntaxins (e.g., STX4, STX1A, STX7) and SNAP23/29 to mediate vesicle fusion .

Key Functional Roles

  • Autophagy: Directs autophagosome-lysosome fusion by binding STX17-SNAP29 complexes .

  • Regulated Secretion: Facilitates dense granule release in platelets , mucin exocytosis in goblet cells , and enzyme secretion in exocrine glands .

  • Immune Response: Mediates cytotoxic granule exocytosis in T-cells and TNF-α release in macrophages .

Immune Synapse Formation and Cytotoxicity

  • Role in Cytotoxic T-Lymphocytes (CTLs):

    • VAMP8 localizes to recycling endosomes rather than cytotoxic granules in human CTLs .

    • Facilitates fusion of recycling endosomes with the plasma membrane, enabling syntaxin-11 delivery for cytotoxic granule exocytosis .

    • Knockdown reduces target cell killing efficiency by ~50% .

Autophagy and Disease Implications

  • Glioma Progression:

    • VAMP8 overexpression correlates with poor prognosis in glioblastoma (HR = 2.1, p < 0.001) .

    • Promotes temozolomide resistance by enhancing autophagic flux (autophagosome count increases by 3-fold in VAMP8-overexpressing cells) .

Autophagy-Related PartnersFunctionReference
STX17Lysosomal fusion
SNAP29SNARE complex assembly
ATG5Autophagosome formation

Mucin Secretion and Intestinal Homeostasis

  • Goblet Cell Exocytosis:

    • VAMP8 knockout mice exhibit 9-fold reduced mucin secretion, leading to compromised intestinal barrier function .

    • Impaired mucin release increases susceptibility to Citrobacter rodentium infection (bacterial load: 10<sup>8</sup> CFU/g in KO vs. 10<sup>5</sup> CFU/g in WT) .

Inflammatory and Immune Disorders

  • Anaphylatoxin-Induced Inflammation:

    • VAMP8-deficient mice show reduced TNF-α secretion (70% decrease) and attenuated neutrophil recruitment .

    • Protects against systemic inflammation (serum IL-6 unaffected) .

Cancer Biomarker Potential

  • Breast Cancer (BC):

    • VAMP8 overexpression correlates with tumor size (>5 cm: 65% vs. 35% in low-VAMP8 tumors), lymph node metastasis (OR = 2.4), and recurrence risk (HR = 3.1) .

    • 5-year survival rates: 42% (high VAMP8) vs. 78% (low VAMP8) .

Disease AssociationMechanistic InsightReference
GliomaAutophagy-mediated chemoresistance
ColitisImpaired mucin barrier function
Sjögren’s Syndrome (proposed)Defective lacrimal gland secretion

Regulatory Mechanisms and Therapeutic Targets

  • miRNA Regulation:

    • miR-96 suppresses VAMP8 mRNA and protein levels by >50% in platelets, modulating thrombotic risk .

  • TRIM6-Dependent Antiviral Response:

    • VAMP8 enhances IFN-I signaling by promoting STAT1 phosphorylation (2-fold increase in IFIT1 expression) .

Product Specs

Introduction
VAMP8, also known as endobrevin, is a key component of the SNARE complex, which plays a crucial role in the docking and fusion of synaptic vesicles with the presynaptic membrane. This protein is involved in regulating enzyme secretion in pancreatic acinar cells and participates in the abscission of the midbody during cell division, ultimately leading to the complete separation of daughter cells. VAMP8 is essential for dense-granule secretion in platelets and is associated with the perinuclear vesicular structures of the early endocytic compartment. It interacts specifically with the soluble NSF-attachment protein (alpha-SNAP) through a VAMP8-containing SNARE complex.
Description
Recombinant Human VAMP8, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 96 amino acids (1-76 a.a.). It has a molecular weight of 10.9 kDa. The VAMP8 protein is fused to a 20 amino acid His Tag at the N-terminus and purified using proprietary chromatography techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The VAMP8 protein solution is provided at a concentration of 0.25 mg/ml in a buffer containing 20mM Tris pH 8, 0.1mM PMSF, 0.2M NaCl, and 50% glycerol.
Stability
For short-term storage (2-4 weeks), the protein should be stored at 4°C. For extended storage, it is recommended to freeze the protein at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 85.0% as determined by SDS-PAGE analysis.
Synonyms
VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.

Product Science Overview

Molecular and Biochemical Characteristics

Endobrevin shares significant sequence identity with other members of the synaptobrevin/VAMP family, including synaptobrevin/VAMP-1, synaptobrevin/VAMP-2, and cellubrevin . The protein is primarily associated with the early endosome, a key compartment in the endocytic pathway .

Functional Role

Endobrevin plays a critical role in the homotypic fusion of secretory granules, particularly in pancreatic acinar cells . This process is essential for the proper delivery and storage of secretory content. The SNARE (Soluble NSF Attachment Protein Receptor) machinery, which includes endobrevin, mediates membrane fusion events required for the granule lifecycle .

Research and Applications

Research has shown that endobrevin interacts with other proteins such as alpha-SNAP (Soluble NSF Attachment Protein) and glutathione S-transferase (GST) in vitro . These interactions highlight the importance of endobrevin in membrane traffic and provide avenues for future functional and mechanistic studies .

Endobrevin has been studied in various cell types, including platelets, basophilic cells, cytotoxic T cells, mast cells, kidney collecting duct cells, and airway goblet cells . These studies have expanded our understanding of the protein’s role in different physiological contexts and its potential implications in health and disease.

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