Animal ID:
RB0047-0048
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Host:
Rabbit
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Reactivity:
human
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Buffers:
Purified rabbit polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column and eluted out with both high and low pH buffers and neutralized immediately after elution then followed by dialysis against PBS.
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Storage:
Maintain refrigerated at 2-8ºC for up to 6 months. For long term storage store at -20ºC. Avoid repeated freeze-thaw cycles.
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Application:
Tested by peptide-specific ELISA (1:1,000).
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Immunogen:
KLH conjugated synthetic peptide comprised of amino acids 1 - 17 [MAESSDKLYRVEYAKSG] of the human ADP-ribosyltransferase (ADPRT) protein.
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Accession number:
NM_001618
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Description:
ADP-ribosyltransferase (ADPRT) is a chromatin-associated enzyme, poly(ADP-ribosyl)transferase, which modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. In addition, ADPRT may be the site of mutation in Fanconi anemia, and may participate in the pathophysiology of type I diabetes. Cenpa, Cenpb, and Bub3, but not Cenpc, interact with ADPRT. Genetic knockout of ADPRT in mice causes medulloblastomas also deficient in p53. ADPRT and ADPRT-mediated poly(ADP-ribosyl)ation of centrosomal proteins are involved in the regulation of centrosome function and ADPRT cleavage functions as a molecular switch between apoptotic and necrotic modes of death receptor-induced cell death. It seems like ADPRT activation causes apoptosis-inducing factor (AIF) release from mitochondria, resulting in a caspase-independent pathway of programmed cell death.
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Alternative Name(s):
poly(ADP-ribosyl)transferase, PARP, PPOL, ADPRT1, PARP-1, pADPRT-1, poly(ADP-ribose) synthetase, ADP-ribosyltransferase NAD(+)
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References:
- Beneke R, Geisen C, Zevnik B, Bauch T, Muller WU, Kupper JH, Moroy T: DNA excision repair and DNA damage-induced apoptosis are linked to Poly(ADP-ribosyl)ation but have different requirements for p53. Mol. Cell. Biol. 20(18): 6695-6703 (2000).
- Vispe S, Yung TM, Ritchot J, Serizawa H, Satoh MS: A cellular defense pathway regulating transcription through poly(ADP-ribosyl)ation in response to DNA damage. Proc. Natl. Acad. Sci. U S A. 97(18): 9886-9891 (2000).
- d'Adda di Fagagna F, Hande MP, Tong WM, Lansdorp PM, Wang ZQ, Jackson SP: Functions of poly(ADP-ribose) polymerase in controlling telomere length and chromosomal stability. Nat. Genet. 23(1): 76-80 (1999).
- Pieper AA, Brat DJ, Krug DK, Watkins CC, Gupta A, Blackshaw S, Verma A, Wang ZQ, Snyder SH: Poly(ADP-ribose) polymerase-deficient mice are protected from streptozotocin-induced diabetes. Proc. Natl. Acad. Sci. U S A. 96(6): 3059-3064 (1999).
- Uchida K, Morita T, Sato T, Ogura T, Yamashita R, Noguchi S, Suzuki H, Nyunoya H, Miwa M, Sugimura T: Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase. Biochem. Biophys. Res. Commun. 148(2): 617-622 (1987).
- Suzuki H, Uchida K, Shima H, Sato T, Okamoto T, Kimura T, Miwa M: Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation. Biochem. Biophys. Res. Commun. 146(2): 403-409 (1987).
- Loetscher P, Alvarez-Gonzalez R, Althaus FR: Poly(ADP-ribose) may signal changing metabolic conditions to the chromatin of mammalian cells. Proc. Natl. Acad. Sci. U S A. 84(5): 1286-1289 (1987).
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For Research Use Only. Not for Diagnostic or Therapeutic Use.
Purchase does not include or carry any right to resell or transfer this product either as a stand-alone product or as a component of another product. Any use of this product other than the permitted use without the express written authorization of Orbigen, Inc. is strictly prohibited
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