Peptide ELISA: antibody detection limit dilution 1: 32000. Western blot: 0.5-2 μg/mL. Approx 60 kDa band observed in Hela, Human Lung and HumanTestis lysates (predicted MW of 60 kDa according to NP_110379.2). Immunohistochemistry: 1-2 μg/mL. In paraffin embedded Human Testis shows onlycytoplasmic staining in some germ cells, and both cytoplasmic and nuclear staining inother germ cells with unstained nucleoli.
TCP1 alpha is a ~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 (HSP 70) 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 TCP1 sequence shows nearly 40 % identity to TF55, but only minimal similarity to HSP60 and GroEL.Synonyms: CCT alpha, CCTA, Chaperonin containing T complex polypeptide 1 subunit 1, T-complex protein 1 subunit alpha, TCP-1-alpha, TCP1 alpha