F0807
Anti-FNTB (276-290) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-FPTB, Anti-Farnesyltransferase subunit β
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About This Item
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~49 kDa
species reactivity
human
technique(s)
western blot: 1:500-1:2,000
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... FNTB(2342)
Immunogen
synthetic peptide corresponding to amino acids 276-290 of human FNTB
Application
Anti-FNTB (276-290) antibody produced in rabbit is suitable for western blotting at a dilution of 1:500-1:2,000.
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.
Yale Center for High Throughput Cell Biology IF-tested antibodies. Each antibody is tested by immunofluorescence against HUVEC cells using the Yale HTCB IF protocol. To learn more about us and Yale Center for High Throughput Cell Biology partnership, visit sigma.com/htcb-if.
Biochem/physiol Actions
Protein farnesyltransferase subunit β is an enzyme encoded by the FNTB gene in humans and is located on human chromosome bands 14q23-q24. It helps in catalyzing the biologically relevant lipidation of cellular proteins. FTase may play an important role in the genesis and development of primary liver cancer (PLC). It may act as a reliable marker for the metastatic activity gained by liver tumor cells. FTase may be used clinically in predicting metastatic recurrence of PLC. Farnesyl protein transferase (FPTase) inhibitors (FTIs) were also developed as potential anticancer agents targeting the ras oncogene and also for parasitic infections.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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James L Hougland et al.
The Journal of biological chemistry, 287(45), 38090-38100 (2012-09-21)
Post-translational modifications play essential roles in regulating protein structure and function. Protein farnesyltransferase (FTase) catalyzes the biologically relevant lipidation of up to several hundred cellular proteins. Site-directed mutagenesis of FTase coupled with peptide selectivity measurements demonstrates that molecular recognition is
T Scott Reid et al.
Biochemistry, 43(22), 6877-6884 (2004-06-02)
The search for new cancer therapeutics has identified protein farnesyltransferase (FTase) as a promising drug target. This enzyme attaches isoprenoid lipids to signal transduction proteins involved in growth and differentiation. The two FTase inhibitors (FTIs), R115777 (tipifarnib/Zarnestra) and BMS-214662, have
R B Lobell et al.
Cancer research, 61(24), 8758-8768 (2001-12-26)
Farnesyl:protein transferase (FPTase) inhibitors (FTIs) were originally developed as potential anticancer agents targeting the ras oncogene and are currently in clinical trials. Whereas FTIs inhibit the farnesylation of Ha-Ras, they do not completely inhibit the prenylation of Ki-Ras, the allele
Guo-de Sui et al.
Chinese medical journal, 125(14), 2427-2431 (2012-08-14)
Primary liver cancer (PLC) is a common malignant tumor. Over the past decade, although farnesyltransferase (FTase) has emerged as a significant target for anticancer therapies and has become a hotspot of cancer research, its exact mechanism of action remains unknown.
D A Andres et al.
Genomics, 18(1), 105-112 (1993-10-01)
The CAAX farnesyltransferase is a heterodimeric enzyme that attaches a farnesyl group to a single cysteine in several cellular proteins. Substrates include the p21ras proteins, nuclear lamins, and several retinal proteins, all of which end with a "CAAXbox," where C
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