KLH-conjugated synthetic peptide encompassing a sequence within the N-term region of human Endobrevin. The exact sequence is proprietary.
Conjugation:
Unconjugated
Alternative Names:
Vesicle-associated membrane protein 8, VAMP-8, Endobrevin, EDB
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) . Vesicle associated membrane protein 8 (VAMP8), also known as endobrevin, is a v-SNARE originally found preferentially localized to early endosomes. VAMP8 knockout mice did not show abnormal endosomal vesicular trafficking, perhaps having a redundant role with other VAMP family members. 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. In addition, lysosome localized VAMP8 has been shown to play a role in autophagosome/lysosome fusion during antimicrobial (xenophagy) and canonical starvation induced autophagy.
