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|Tested species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||KLH conjugated synthetic peptide between 6-36 amino acids from the N-terminal region of human FNTB|
|Purification||Size-exclusion - Dialysis, Ammonium sulfate precipitation|
|Contains||0.09% sodium azide|
|Storage Conditions||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody is predicted to react with bovine and rat based on sequence homology.
Eukaryotic cells contain 3 different types of prenyltransferases that attach either a farnesyl group (15 carbons) or a geranylgeranyl group (20 carbons) in thioether linkage to C-terminal cysteine residues in a variety of proteins. These posttranslational modifications provide a mechanism for membrane localization of proteins that lack a transmembrane domain. 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 CAAX box, where C is cysteine, A is usually but not always an aliphatic amino acid, and X is typically methionine or serine. This enzyme has the ability to farnesylate peptides as short as 4 residues in length that conform to the CAAX consensus sequence. The gene for the beta subunit of CAAX farnesyltransferase (FNTB) has been pinpointed to 14q23-q24 by Southern blot hybridization and PCR analyses of panels of human/Chinese hamster somatic cell hybrid lines and by fluorescence chromosomal in situ hybridization.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
CAAX farnesyltransferase subunit beta; EC 126.96.36.199; FNTB; FTase-beta; RAS proteins prenyltransferase beta; ras proteins prenyltransferase subunit beta