Render Target: STATIC
Render Timestamp: 2024-12-20T11:12:18.135Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-09-20 06:14:39.748
Product last modified at: 2024-11-14T13:15:31.599Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

VAMP8 Antibody #13060

Filter:
  • WB

    Supporting Data

    REACTIVITY H M
    SENSITIVITY Endogenous
    MW (kDa) 15
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    VAMP8 Antibody recognizes endogenous levels of total VAMP8 protein.

    Species Reactivity:

    Human, Mouse

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Monkey, Dog

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val31 of human VAMP8 protein. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Proteins in the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex are integral membrane proteins involved in vesicle transport and membrane fusion by pairing of vesicular SNAREs (v-SNAREs) with cognate target SNAREs (t-SNAREs) (reviewed in 1,2). Vesicle associated membrane protein 8 (VAMP8), also known as endobrevin, is a v-SNARE originally found preferentially localized to early endosomes (3). VAMP8 knockout mice did not show abnormal endosomal vesicular trafficking, perhaps having a redundant role with other VAMP family members (4). Instead, research studies have shown that VAMP8 is widely expressed in exocrine tissues and has a critical role in the exocytosis pathways of a variety of cells (4-9). In addition, lysosome localized VAMP8 has been shown to play a role in autophagosome/lysosome fusion during antimicrobial (xenophagy) and canonical starvation induced autophagy (5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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