CAMK1D Antibody – Rabbit Polyclonal

This gene is a member of the calcium/calmodulin-dependent protein kinase 1 family, a subfamily of the serine/threonine kinases. The encoded protein is a component of the calcium-regulated calmodulin-dependent protein kinase cascade. It has been associated with multiple processes including regulation of granulocyte function, activation of CREB-dependent gene transcription, aldosterone synthesis, differentiation and activation of neutrophil cells, and apoptosis of erythroleukemia cells. Alternatively spliced transcript variants encoding different isoforms of this gene have been described. [provided by RefSeq, Jan 2015]

CAMK1D: a calcium/calmodulin-dependent S/T protein kinase of the CAMK group. Binding of calmodulin is thought to result in a conformational change and can lead to subsequent activation through phosphorylation by CAMKK1 and CAMKK2. Can be activated by CAMKK1 in a calcium-independent manner. Its Ca(2+)/CaM-dependent activity is enhanced 30-fold in vitro by phosphorylation at Thr180 by CaMKK1. Broadly expressed. Highly and mostly expressed in polymorphonuclear leukocytes (neutrophilic and eosinophilic granulocytes) while little or no expression is observed in monocytes and lymphocytes. May regulate calcium-mediated granulocyte function. May play a role in apoptosis of erythroleukemia cells. In vitro, phosphorylates transcription factor CREM isoform Beta and probably CREB1. Expression increases upon treatment of EC cells with DMSO and retinoic acid. Two isoforms of the human protein are produced by alternative splicing.

Protein type: Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Protein kinase, CAMK; EC 2.7.11.17; CAMK group; CAMK1 family

Chromosomal Location of Human Ortholog: 10p13

Cellular Component: cytoplasm; nucleus

Molecular Function: calmodulin binding; calmodulin-dependent protein kinase activity; ATP binding

Biological Process: positive regulation of apoptosis; positive regulation of phagocytosis; activation of CREB transcription factor; regulation of dendrite development; inflammatory response; protein amino acid phosphorylation; negative regulation of apoptosis