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Notch 1 (NOTCH1) (N-Term) antibody

Details for Product No. ABIN966681
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Antigen
Synonyms notch1, NOTCH1, hn1, tan1, notch, xotch, xnotch, notch-1, xnotch1, TAN1, hN1, 9930111A19Rik, Mis6, N1, Tan1, lin-12, NOTCH, Xotch, notch1-a
Epitope
N-Term
(29), (19), (17), (7), (6), (5), (5), (3), (3), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(116), (90), (30), (3), (2), (1), (1), (1), (1)
Host
Rabbit
(88), (75), (5), (4), (3), (2)
Clonality
Polyclonal
Conjugate
Un-conjugated
(10), (8), (4), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (IHC)
(110), (52), (47), (35), (33), (26), (16), (10), (6), (2), (1), (1)
Pubmed 7 references available
Quantity 0.1 mg
Options
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Catalog No. ABIN966681
452.38 $
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to very N-terminal residues of human NOTCH1 (Neurogenic locus notch homolog protein 1)
Alternative Name NOTCH1
Background NOTCH1 (Neurogenic locus notch homolog protein 1) 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. NOTCH1 affects the implementation of differentiation, proliferation and apoptotic programs. NOTCH1 may be important for normal lymphocyte function. In altered form, NOTCH1 may contribute to transformation or progression in some T-cell neoplasms. NOTCH1 is involved in the maturation of both CD4+ and CD8+ cells in the thymus. NOTCH1 may be important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, may function as a receptor for neuronal DNER and may be involved in the differentiation of Bergmann glia. 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.
Synonyms: TAN1(Translocation-associated notch protein TAN-1)
Restrictions For Research Use only
Product cited in: Ellisen, Bird, West et al.: "TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms." in: Cell, Vol. 66, Issue 4, pp. 649-61, 1991 (PubMed).

Matsuno, Eastman, Mitsiades et al.: "Human deltex is a conserved regulator of Notch signalling." in: Nature genetics, Vol. 19, Issue 1, pp. 74-8, 1998 (PubMed).

Gray, Mann, Mitsiadis et al.: "Human ligands of the Notch receptor." in: The American journal of pathology, Vol. 154, Issue 3, pp. 785-94, 1999 (PubMed).

Wu, Aster, Blacklow et al.: "MAML1, a human homologue of Drosophila mastermind, is a transcriptional co-activator for NOTCH receptors." in: Nature genetics, Vol. 26, Issue 4, pp. 484-9, 2000 (PubMed).

Wu, Sun, Kobayashi et al.: "Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors." in: Molecular and cellular biology, Vol. 22, Issue 21, pp. 7688-700, 2002 (PubMed).

Vardar, North, Sanchez-Irizarry et al.: "Nuclear magnetic resonance structure of a prototype Lin12-Notch repeat module from human Notch1." in: Biochemistry, Vol. 42, Issue 23, pp. 7061-7, 2003 (PubMed).

Hambleton, Valeyev, Muranyi et al.: "Structural and functional properties of the human notch-1 ligand binding region." in: Structure (London, England : 1993), Vol. 12, Issue 12, pp. 2173-83, 2004 (PubMed).

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