344145
FPTase, Rat, Recombinant, E. coli
A heterodimeric enzyme that catalyzes the transfer of a 15-carbon isoprenoid group to a variety of cellular proteins including Ras.
Sinónimos:
Farnesyl Proteintransferase, FTase
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About This Item
Productos recomendados
recombinant
expressed in E. coli
Quality Level
assay
≥85% (SDS-PAGE)
form
liquid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
shipped in
wet ice
storage temp.
−70°C
General description
M.W. α-subunit: ~48,000; β-subunit: ~46,000
Recombinant, rat FPTase expressed in E. coli. A heterodimeric enzyme that catalyzes the transfer of a 15-carbon isoprenoid group to a C-terminal cysteine in a variety of cellular proteins, including Ras. Recognizes the CaaX motif where the farnesylated cysteine (C) is followed by two aliphatic amino acids (aa) and either leucine or serine (X). Expressed in E. coli as an untagged recombinant protein.
Recombinant, rat FPTase expressed in E. coli. A heterodimeric enzyme that catalyzes the transfer of a 15-carbon isoprenoid group to a variety of cellular proteins including Ras. Recognizes the C-terminal CAAX cysteine motif where the farnesylated cysteine is followed by two aliphatic amino acids and either leucine or serine.
Biochem/physiol Actions
1 pmol of FPTase will transfer 1 pmol of farnesyl to H-Ras in 15 min at 37°C.
Warning
Toxicity: Standard Handling (A)
Physical form
In 25 mM HEPES, pH 7.2, 40 mM NaCl, 5µM ZnCl2, and 1mM TECP
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Other Notes
Hightower, K.E., et al. 2001. Biochem. J.360, 625.
Zimmerman, K.K., et al. 1998. Protein Expr. Purif.14, 395.
Reiss, Y., et al. 1990. Cell62, 81.
Zimmerman, K.K., et al. 1998. Protein Expr. Purif.14, 395.
Reiss, Y., et al. 1990. Cell62, 81.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
10 - Combustible liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Advanced science (Weinheim, Baden-Wurttemberg, Germany), 8(23), e2102414-e2102414 (2021-10-20)
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