|Other Names||Neurogenic locus notch homolog protein 1, Notch 1, hN1, Translocation-associated notch protein TAN-1, Notch 1 extracellular truncation, NEXT, Notch 1 intracellular domain, NICD, NOTCH1, TAN1|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6218a was selected from the C-term region of human NOTCH1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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.|
|Function||Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. 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. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4+ and CD8+ cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO).|
|Cellular Location||Cell membrane; Single-pass type I membrane protein|
|Tissue Location||In fetal tissues most abundant in spleen, brain stem and lung. Also present in most adult tissues where it is found mainly in lymphoid tissues|
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NOTCH1 functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBP-J kappa and activates genes of the enhancer of split locus. This protein effects the implementation of differentiation, proliferation and apoptotic programs, and may be important for normal lymphocyte function. In altered form, it may contribute to transformation or progression in some T-cell neoplasms. In fetal tissues it is most abundant in spleen, brain stem and lung. NOTCH1 is also present in most adult tissues where it is found mainly in lymphoid tissues. NOTCH1 is synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane NOTCH1 truncation is associated with T-cell acute lymphoblastic leukemia. NOTCH1 contains a putative 5 ANK repeats and 36 EGF-like domains.
Gray, G.E., et al., Am. J. Pathol. 154(3):785-794 (1999).Matsuno, K., et al., Nat. Genet. 19(1):74-78 (1998).Ellisen, L.W., et al., Cell 66(4):649-661 (1991).
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