Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical α and β subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The β subunit, which is known as FTβ, CAAX farnesyltransferase subunit β, or Ras proteins prenyltransferase subunit β, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The α subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.
Background References
1. Villalobos, X. et al. 2014. Stability and immunogenicity properties of the gene-silencing polypurine reverse Hoogsteen hairpins. Molecular pharmaceutics. 11: 254-64.
2. Yang, G. et al. 2013. RAS promotes tumorigenesis through genomic instability induced by imbalanced expression of Aurora-A and BRCA2 in midbody during cytokinesis. Int. J. Cancer. 133: 275-285.
Sequence Similarity
Belongs to the protein prenyltransferase subunit beta family.
Western blot analysis of FNTB on different lysates with Rabbit anti-FNTB antibody (ET1610-99) at 1/5,000 dilution.
Lane 1: K-562 cell lysate (15 µg/Lane) Lane 2: JAR cell lysate (15 µg/Lane) Lane 3: Rat brain tissue lysate (30 µg/Lane)
Predicted band size: 49 kDa Observed band size: 49 kDa
Exposure time: 1 minute; ECL: K1801;
4-20% SDS-PAGE gel.
Proteins were transferred to a PVDF membrane and blocked with 5% NFDM/TBST for 1 hour at room temperature. The primary antibody (ET1610-99) at 1/5,000 dilution was used in primary antibody dilution (K1803) at 4℃ overnight. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1/50,000 dilution was used for 1 hour at room temperature.
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