DISC1 antibody (Disrupted in Schizophrenia 1) (N-Term)

Details for Product anti-DISC1 Antibody No. ABIN965999, Supplier: Log in to see
Antigen
  • DISC1
  • C1orf136
  • SCZD9
  • disrupted in schizophrenia 1
  • disc1
  • DISC1
  • Disc1
Alternatives
anti-Human DISC1 antibody for ELISA
Epitope
N-Term
47
47
18
17
17
14
9
5
5
5
5
2
2
2
2
2
1
1
1
1
1
Reactivity
Human
153
78
52
1
Host
Rabbit
156
15
13
3
Clonality
Polyclonal
Conjugate
This DISC1 antibody is un-conjugated
9
9
7
4
4
3
3
3
3
3
3
2
2
2
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC)
140
76
62
58
29
26
25
14
12
7
6
3
1
Options
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human DISC1 (Disrupted in schizophrenia 1 protein)
Purification Purified by antigen-specific affinity chromatography.
Alternative Name DISC1 (Disrupted in schizophrenia 1 protein) (DISC1 Antibody Abstract)
Background Disrupted-In-Schizophrenia 1 (DISC1) is associated with schizophrenia by multiple genetic studies. DISC1 might cause susceptibility to schizophrenia. DISC1 has distinct interaction domains: MAP1A interacts via its LC2 domain with the N-terminus of DISC1, whereas MIPT3 and NUDEL bind via their C-terminal domains to the central coiled-coil domain of DISC1, and ATF4/5 bind via their C-terminal domains to the C-terminus of DISC1. DISC1 protein localizes to predominantly perinuclear punctate structures which extend into neurites in some cells. DISC1 is a multifunctional protein whose truncation contributes to schizophrenia susceptibility by disrupting intracellular transport, neurite architecture and/or neuronal migration, all of which have been hypothesized to be pathogenic in the schizophrenic brain. DISC1 interacts with Nudel through a leucine zipper domain and binds to a novel DISC1-interaction domain on Nudel, which is independent from the Lis1 binding site. Nudel is able to act as a bridge between DISC1 and Lis1 to allow formation of a trimolecular complex. Nudel has been implicated to play a role in neuronal migration, together with the developmental variation in the abundance of the DISC1-Nudel complex, may implicate a defective DISC1-Nudel complex as a neurodevelopmental cause of schizophrenia.
Pathways Regulation of Cell Size
Application Notes ELISA, Western blotting: 1µg/ml for 2hrs.
Restrictions For Research Use only
Format Liquid
Buffer This antibody is stored in PBS, 50% glycerol
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Lipska, Peters, Hyde, Halim, Horowitz, Mitkus, Weickert, Matsumoto, Sawa, Straub, Vakkalanka, Herman, Weinberger, Kleinman: "Expression of DISC1 binding partners is reduced in schizophrenia and associated with DISC1 SNPs." in: Human molecular genetics, Vol. 15, Issue 8, pp. 1245-58, 2006 (PubMed).

Brandon, Schurov, Camargo, Handford, Duran-Jimeniz, Hunt, Millar, Porteous, Shearman, Whiting: "Subcellular targeting of DISC1 is dependent on a domain independent from the Nudel binding site." in: Molecular and cellular neurosciences, Vol. 28, Issue 4, pp. 613-24, 2005 (PubMed).

Brandon, Handford, Schurov, Rain, Pelling, Duran-Jimeniz, Camargo, Oliver, Beher, Shearman, Whiting: "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders." in: Molecular and cellular neurosciences, Vol. 25, Issue 1, pp. 42-55, 2004 (PubMed).

Morris, Kandpal, Ma, Austin: "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation." in: Human molecular genetics, Vol. 12, Issue 13, pp. 1591-608, 2003 (PubMed).

Ozeki, Tomoda, Kleiderlein, Kamiya, Bord, Fujii, Okawa, Yamada, Hatten, Snyder, Ross, Sawa: "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, Issue 1, pp. 289-94, 2003 (PubMed).