|Reactivity||Human, Mouse, Rat|
|Calculated MW||211067 Da|
|Other Names||Plexin-A1, Semaphorin receptor NOV, PLXNA1, NOV, PLXN1|
|Target/Specificity||A synthetic peptide corresponding to residues in human Plexin-A1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Plexin-A1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down- stream signaling events in the cytoplasm (By similarity).|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Detected in fetal brain, lung, liver and kidney.|
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Provided below are standard protocols that you may find useful for product applications.
Plexins are large transmembrane receptors for semaphorins. It contains a sema domain and a highly conserved cytoplasmic domain (1). Plexins are classified into four groups: A, B, C, D. Plexin-A1 is a co-receptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. It is necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plexin-A1 plays a role in axon guidance, invasive growth and cell migration. Plexin-A1 modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (2). Plexin-A1 is specific in fetal brain, lung, liver and kidney (3).
1. Artigianis, et al. EMBO Reports 5,7:710-714 (2004) 2. The UniProt Consortium, The Universal Protein Resource (UniProt), Nucleic Acids Res. 36:D190-D195 (2008). 3. Tamagnone L, et al. Cell 99(1):71-80, 1999
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