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Human TWF1 / PTK9 / Twinfilin-1 Protein

A6,MGC23788,MGC41876,PTK9

Catalog Number P11829-HNCE
Organism Species Human
Host E. coli
Synonyms A6,MGC23788,MGC41876,PTK9
Molecular Weight The recombinant human TWF1 consists of 254 amino acids and has a calculated molecular mass of 29 kDa. It migrates as an approximately 36 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 94 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human TWF1 isoform 4 (Q12792-4) (Met 1-Asp 252) was expressed and purified, with additional two amino acids (Gly & Pro) at the N-terminus.
Bio-activity
Research Area Cancer |Signal transduction |Protein Kinase |Intracellular Kinase |Other Intracellular Protein Kinases
Formulation Lyophilized from sterile PBS, pH 7.4, 10% glycerol
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Twinfilin-1, also known as Protein A6, Protein tyrosine kinase 9, TWF1 and PTK9, is a cytoplasm protein which belongs to the actin-binding proteins ADF family and Twinfilin subfamily. Twinfilin-1 (TWF1 / PTK9 ) is a highly conserved actin monomer-binding protein that regulates cytoskeletal dynamics in organisms from yeast to mammals. In addition to the mammalian twinfilin-1, a second protein with approximately 65% sequence identity to twinfilin-1 exists in mouse and humans. TWF1 / PTK9 is expressed at high levels in the colon, testis, ovary, prostate and lung. It is expressed at lower levels in the brain, bladder and heart. It is not detected in liver. TWF1 / PTK9 is an actin-binding protein involved in motile and morphological processes. It inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. TWF1 / PTK9 seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.
Reference
  • Beeler JF, et al.,1994, Mol Cell Biol 14 (2): 982-8.
  • Palmgren S, et al., 2002, J. Cell. Sci. 115 (Pt 5): 881-6.
  • Vartiainen MK, et al.,2003, J. Biol. Chem. 278 (36): 34347-55.
  • Hassel S, et al.,2004, Proteomics 4 (5): 1346-58.
  • Moseley,J.B. et al., 2006, J Cell Sci. 119 (Pt 8):1547-57.