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1 µg/mL of MA5-45715 was sufficient for detection of TCP1 alpha in 20 µg of 3T3 cell lysate by colorimetric immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody.|Detects approximately 60kDa. Also detects approximately 92kDa. The addition of an alanine (LDDA COOH) prevents binding in ELISA assays to immobilized synthetic peptide sequences. This antibody recognizes other proteins, most notably the p102B' COP subunit of Golgi coatomer. It does not react with human HSP60 protein.
The T Complex Polypeptide 1 (TCP-1) is approximately 60 kDa protein constitutively expressed in almost all eukaryotic cells, and is upregulated during spermatogenesis. It is found in the cytosol as a subunit of a hetero-oligomeric chaperone that is known to be involved in the folding of actin and tubulin. The family of proteins termed chaperonins act to recognize and stabilize polypeptide intermediates during folding, assembly and disassembly, and share many characteristics with Heat Shock Protein 70 (HSP70) including high abundance, induction by environmental stress, and ATPase activity. The chaperonin family includes the mitochondrial HSP60, Escherichia coli GroEL, the plastid Rubisco-subunit binding protein, and the archaebacterial protein TF55. The TCP-1 sequence shows nearly 40% identity to TF55, but only minimal similarity to HSP60 and GroEL.
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