- CITATIONS: 1
|Application ||WB, IHC-P, IF, E|
|Calculated MW||243631 Da|
|Antigen Region||2291-2321 aa|
|Other Names||Neurogenic locus notch homolog protein 3, Notch 3, Notch 3 extracellular truncation, Notch 3 intracellular domain, NOTCH3|
|Target/Specificity||This NOTCH3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 2291-2321 amino acids from the C-terminal region of human NOTCH3.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|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||NOTCH3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination (PubMed:15350543). Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity).|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||Ubiquitously expressed in fetal and adult tissues|
Provided below are standard protocols that you may find useful for product applications.
NOTCH3 is the third discovered human homologue of the Drosophilia melanogaster type I membrane protein notch. In Drosophilia, notch interaction with its cell-bound ligands (delta, serrate) establishes an intercellular signalling pathway that plays a key role in neural development. Homologues of the notch-ligands have also been identified in human, but precise interactions between these ligands and the human notch homologues remains to be determined. Mutations in NOTCH3 have been identified as the underlying cause of cerebral autosomal dominant arteriopathy with subcortical infarcts and leukoencephalopathy (CADASIL).
Suwanwela, N., et al., J Med Assoc Thai 86(2):178-182 (2003). Ahearn, E.P., et al., Am. J. Med. Genet. 114(6):652-658 (2002). Bellavia, D., et al., Proc. Natl. Acad. Sci. U.S.A. 99(6):3788-3793 (2002). Ito, D., et al., J. Neurol. Neurosurg. Psychiatr. 72(3):382-384 (2002). Joutel, A., et al., Lancet 350(9090):1511-1515 (1997).
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