This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This ADPRH antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 306-334 amino acids from the C-terminal region of human ADPRH.
ADPRH
Reaktivität: Human
WB, ELISA
Wirt: Kaninchen
Polyclonal
FITC
Applikationshinweise
WB: 1:1000
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Haltbarkeit
6 months
Kernstock, Koch-Nolte, Mueller-Dieckmann, Weiss, Mueller-Dieckmann: "Cloning, expression, purification and crystallization as well as X-ray fluorescence and preliminary X-ray diffraction analyses of human ADP-ribosylhydrolase 1." in: Acta crystallographica. Section F, Structural biology and crystallization communications, Vol. 65, Issue Pt 5, pp. 529-32, (2009) (PubMed).
Lamesch, Li, Milstein, Fan, Hao, Szabo, Hu, Venkatesan, Bethel, Martin, Rogers, Lawlor, McLaren, Dricot, Borick, Cusick, Vandenhaute, Dunham, Hill, Vidal: "hORFeome v3.1: a resource of human open reading frames representing over 10,000 human genes." in: Genomics, Vol. 89, Issue 3, pp. 307-15, (2007) (PubMed).
Weber, Aldred, Morrison, Plass, Frilling, Broelsch, Waite, Eng: "Silencing of the maternally imprinted tumor suppressor ARHI contributes to follicular thyroid carcinogenesis." in: The Journal of clinical endocrinology and metabolism, Vol. 90, Issue 2, pp. 1149-55, (2005) (PubMed).
Glowacki, Braren, Firner, Nissen, Kühl, Reche, Bazan, Cetkovic-Cvrlje, Leiter, Haag, Koch-Nolte: "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse." in: Protein science : a publication of the Protein Society, Vol. 11, Issue 7, pp. 1657-70, (2002) (PubMed).
The enzyme encoded by this gene catalyzes removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. Unlike the rat and mouse enzymes, which require DTT for maximal activity, the human enzyme is DTT-independent.