|Application ||WB, E|
|Other Accession||Q8C985, D0PRN4, Q07310, Q6P9K9, Q9Y4C0, D0PRN3, NP_620426.2|
|Predicted||Chicken, Mouse, Rat|
|Calculated MW||69305 Da|
|Antigen Region||436-462 aa|
|Other Names||Neurexin-3-beta, Neurexin III-beta, Neurexin-3-beta, soluble form, Neurexin-3-beta, C-terminal fragment, NRXN3-CTF, NRXN3, KIAA0743|
|Target/Specificity||This NRXN3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 436-462 amino acids from the C-terminal region of human NRXN3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NRXN3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May play a role in angiogenesis (By similarity).|
|Cellular Location||Membrane; Single-pass type I membrane protein|
|Tissue Location||Expressed in the blood vessel walls (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Neurexins are a family of proteins that function in the vertebrate nervous system as cell adhesion molecules and receptors. They are encoded by several unlinked genes of which two, NRXN1 and NRXN3, are among the largest known human genes. Three of the genes (NRXN1-3) utilize two alternate promoters and include numerous alternatively spliced exons to generate thousands of distinct mRNA transcripts and protein isoforms. The majority of transcripts are produced from the upstream promoter and encode alpha-neurexin isoforms; a much smaller number of transcripts are produced from the downstream promoter and encode beta-neurexin isoforms. The alpha-neurexins contain epidermal growth factor-like (EGF-like) sequences and laminin G domains, and have been shown to interact with neurexophilins. The beta-neurexins lack EGF-like sequences and contain fewer laminin G domains than alpha-neurexins. [provided by RefSeq].
Saus, E., et al. J Psychiatr Res 44(14):971-978(2010)
Hotta, K., et al. J. Hum. Genet. (2010) In press :
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Cirulli, E.T., et al. Eur. J. Hum. Genet. 18(7):815-820(2010)
Novak, G., et al. World J. Biol. Psychiatry 10 (4 PT 3), 929-935 (2009) :
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