PPP3CB Rabbit Polyclonal Antibody (HA500370)

UNIPROT #

P16298

PROTEIN NAME

PPP3CB

SYNONYMS

Calcineurin A beta antibody;Calcineurin A2 antibody;Calcineurin B, formerly antibody;Calmodulin dependent calcineurin A subunit beta isoform antibody;Calmodulin-dependent calcineurin A subunit beta isoform antibody;CALNA 2 antibody;CALNA2 antibody;CALNB antibody;CAM PRP catalytic subunit antibody;CAM-PRP catalytic subunit antibody;CNA2 antibody;CnAbeta antibody;PP2BB_HUMAN antibody;PP2Bbeta antibody;PPP3CB antibody;Protein phosphatase 2B, catalytic subunit, beta isoform, formerly antibody;Protein phosphatase 3 (formerly 2B) catalytic subunit beta isoform antibody;Protein phosphatase 3 catalytic subunit beta isoform antibody;Protein phosphatase 3 catalytic subunit beta isozyme antibody;Serine/threonine protein phosphatase 2B catalytic subunit beta isoform antibody;Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform antibody

SUBCELLULAR LOCATION

Cytoplasm

FUNCTION

Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca2+-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. Negatively regulates MAP3K14/NIK signaling via inhibition of nuclear translocation of the transcription factors RELA and RELB (By similarity). May play a role in skeletal muscle fiber type specification (By similarity). Unlike for protein substrates, PPP3CB activity towards synthetic phosphatase substrate p-nitrophenyl phosphate (pNPP) is increased in presence of the immunosuppressant complex FKBP12-FK506. Activated by Ca2+-bound calmodulin following an increase in intracellular Ca2+. At low Ca2+ concentrations, the catalytic subunit (also known as calcineurin A) is inactive and is bound to the regulatory subunit (also known as calcineurin B) in which only two high-affinity binding sites are occupied by Ca2+. In response to elevated calcium levels, the occupancy of the low-affinity sites on calcineurin B by Ca2+ causes a conformational change of the C-terminal regulatory domain of calcineurin A, resulting in the exposure of the calmodulin-binding domain and in the partial activation of calcineurin A. The subsequent binding of Ca2+-bound calmodulin leads to the displacement of the autoinhibitory domain from the active site and possibly of the autoinhibitory segment from the substrate binding site which fully activates calcineurin A.