Protein geranylgeranyltransferase type I
rat, recombinant, E. coli
α- and β-subunit
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For general laboratory use.
Shipping: shipped on dry ice
Storage Conditions: store at -80 °C
avoid freeze/thaw cycles
Shelf Life: 12 months
Molecular Weight: α: 44 kDa, β: 38 kDa
Accession number: NM_031082
Purity: > 90 % (SDS-PAGE)
Form: liquid (Supplied in 50 mM HEPES pH 7.4, 40 mM NaCl, 1 mM TECP and 5 μM ZnCl2)
Activity: 1 pmol of GGTase-I will transfer 5 pmol of Farnesyl to RhoA in 15 min at 37°C.
GGTase-I (Geranylgeranyltransferase-I) catalyzes the transfer of the farnesyl and geranylgeranyl groups from farnesyl and geranylgeranyl-diphosphate to proteins containing a C-terminal CaaX motif, where 'C' is a conserved cysteine that is the site of farnesyl modification, 'a' is usually an aliphatic amino acid, and 'X' is leucine or phenylalanine.
Farnesyltransferase (FT) and GGTase-I are closely related, sharing a common α subunit and 30% identity in their β subunits.
BIOZ Product Citations:
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Eckert et al. (2009) Regulation of the brain isoprenoids farnesyl- and geranylgeranylpyrophosphate is altered in male Alzheimer patients. Neurobiology of Disease 35 (2):251-257.
Watanabe et al. (2008) Inhibitors of Protein Geranylgeranyltransferase I and Rab Geranylgeranyltransferase Identified from a Library of Allenoate-derived Compounds. J. Biol. Chem. 283 (15):9571-9579.
Hooff et al. (2008) Isoprenoid quantitation in human brain tissue: a validated HPLCfluorescence detection method for endogenous farnesyl- (FPP) and geranylgeranylpyrophosphate (GGPP). Analytical and Bioanalytical Chemistry. 392 (4):673-680.
Lackner et al. (2005) Chemical genetics indentifies Rab geranylgeranyl transferase as an apoptotic target of farnesyl transferase inhibitors. Cancer Cell. 7:325.
Yokoyama et al. (1993) Purification of a mammalian protein geranylgeranyltransferase. Formation and catalytic properties of an enzyme-geranylgeranyl pyrophosphate complex. J. Biol. Chem. 268:4055.