|Application ||WB, E|
|Other Accession||Q04631, Q61239, NP_002018.1|
|Calculated MW||44409 Da|
|Antigen Region||51-79 aa|
|Other Names||Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha, CAAX farnesyltransferase subunit alpha, FTase-alpha, Ras proteins prenyltransferase subunit alpha, Type I protein geranyl-geranyltransferase subunit alpha, GGTase-I-alpha, FNTA|
|Target/Specificity||This FNTA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 51-79 amino acids from the N-terminal region of human FNTA.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||FNTA Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.|
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Provided below are standard protocols that you may find useful for product applications.
Prenyltransferases can attach either a farnesyl group or a geranylgeranyl group in thioether linkage to the cysteine residue of proteins with a C-terminal CAAX box. CAAX geranylgeranyltransferase and CAAX farnesyltransferase are heterodimers that share the same alpha subunit but have different beta subunits. This gene encodes the alpha subunit of these transferases. Alternative splicing results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 11 and 13.
Lipkin, S.M., et al. Cancer Prev Res (Phila Pa) 3(5):597-603(2010)
Fontaine-Bisson, B., et al. J. Mol. Med. 88(2):193-201(2010)
Zhou, J., et al. J. Biol. Chem. 284(15):9648-9655(2009)
Veluthakal, R., et al. Diabetes 56(1):204-210(2007)
Armstrong, S.A., et al. J. Biol. Chem. 270(14):7864-7868(1995)
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