1. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing. 2. Source of all serum proteins is from USDA inspected abattoirs located in the United States. 3. Since applications vary, each investigator should titrate the reagent to obtain optimal results. 4. Please refer to us for technical protocols.
Purification
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
-20 °C
Stockage commentaire
Store undiluted at -20° C.
Saunders, Jurecic, Barber: "The 90- and 110-kDa human NFAR proteins are translated from two differentially spliced mRNAs encoded on chromosome 19p13." dans: Genomics, Vol. 71, Issue 2, pp. 256-9, (2001) (PubMed).
Xu, Grabowski: "Molecular cloning and characterization of a translational inhibitory protein that binds to coding sequences of human acid beta-glucosidase and other mRNAs." dans: Molecular genetics and metabolism, Vol. 68, Issue 4, pp. 441-54, (2000) (PubMed).
Buaas, Lee, Edelhoff, Disteche, Braun: "Cloning and characterization of the mouse interleukin enhancer binding factor 3 (Ilf3) homolog in a screen for RNA binding proteins." dans: Mammalian genome : official journal of the International Mammalian Genome Society, Vol. 10, Issue 5, pp. 451-6, (1999) (PubMed).
Patel, Vestal, Xu, Bandyopadhyay, Guo, Erme, Williams, Sen: "DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR." dans: The Journal of biological chemistry, Vol. 274, Issue 29, pp. 20432-7, (1999) (PubMed).
The double stranded RNA (dsRNA)-dependent, Ser/Thr protein kinase, PKR, is encoded by an IFN-inducible gene and is critical for the anti-viral responses mediated by IFN. Interaction with activators such as heparin, dsRNA, and the dsRNA-binding proteins (DRBPs), DRBP76, PACT, and RAX, induces PKR autophosphorylation and activation. DRBP76 was identified through its binding to dsRNA and PKR. In addition, DRBP76 has been identified as the alternatively spliced nuclear phosphoproteins of 90 kDa (NFAR-1/NF90) and 110 kDa (NFAR-2), as well as M-phase phosphoprotein (MPP4), translational control protein 80 (TCP80), and interleukin enhancer binding factor 3 (ILF3). DRBP76 contains a bi-partite nuclear localization signal at amino acids 369-373 and 386-394, two DRB domains in the C-terminal half, and a C-terminal RG2 domain that is present in many RNA binding proteins. DRBP76 binds pre-mRNAs and spliced mRNAs, co-localizes with PKR in the nucleus, and is phosphorylated by PKR and possibly cyclin-dependent kinases. Thus, DRBP76 may be one of multiple DRBP variants, which associate with PKR and regulate RNA translation. This antibody is routinely tested by western blot analysis.