AVIL Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O75366 |
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Gene ID | 10677 |
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Other Names | Advillin, p92, AVIL |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | AVIL (HGNC:14188) |
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Function | Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling (PubMed:29058690). May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis. In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (PubMed:29058690). |
Cellular Location | Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell junction, focal adhesion. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F- actin-enriched cell periphery that generates lamellipodia and focal adhesions. |
Tissue Location | Most highly expressed in the small intestine and colonic lining. Weaker expression also detected in the thymus, prostate, testes and uterus (PubMed:12034507). Expressed in podocytes (at protein level) (PubMed:29058690). |
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Provided below are standard protocols that you may find useful for product applications.
Background
AVIL is a member of the gelsolin/villin family of actin regulatory proteins. This protein has structural similarity to villin. It binds actin and may play a role in the development of neuronal cells that form ganglia.
References
Piana, S., et al. J. Mol. Biol. 375(2):460-470(2008)Vermeulen, W., et al. Protein Sci. 13(5):1276-1287(2004)Tumer, Z., et al. Gene 288 (1-2), 179-185 (2002)
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