Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Homologie
B, M, Rat
Aufreinigung
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
This FNTA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 330-360 amino acids from the C-terminal region of human FNTA.
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
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Wang, Danielson, Li, Shah, Kim, Donahoe: "The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling." in: Science (New York, N.Y.), Vol. 271, Issue 5252, pp. 1120-2, (1996) (PubMed).
Zhang, Diehl, Kohl, Gibbs, Giros, Casey, Omer: "cDNA cloning and expression of rat and human protein geranylgeranyltransferase type-I." in: The Journal of biological chemistry, Vol. 269, Issue 5, pp. 3175-80, (1994) (PubMed).
Andres, Milatovich, Ozçelik, Wenzlau, Brown, Goldstein, Francke: "cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences." in: Genomics, Vol. 18, Issue 1, pp. 105-12, (1994) (PubMed).
Omer, Kral, Diehl, Prendergast, Powers, Allen, Gibbs, Kohl: "Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases." in: Biochemistry, Vol. 32, Issue 19, pp. 5167-76, (1993) (PubMed).
FNTA, also known as CAAX farnesyltransferase (FTase), attaches a farnesyl group from farnesyl pyrophosphate to cysteine residues at the fourth position from the C terminus of proteins that end in the so-called CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This type of posttranslational modification provides a mechanism for membrane localization of proteins that lack a transmembrane domain. This enzyme has the remarkable property of farnesylating peptides as short as four residues in length that conform to the CAAX consensus sequence. FNTA is also a specific cytoplasmic interactor of the transforming growth factor-beta and activin type I receptors. It is likely to be a key component of the signaling pathway which involves p21ras, an important substrate for farnesyltransferase.