Rabbit anti-Human DAPK2 Polyclonal Antibody

Uniprot Id

Q9UIK4

Target Species

Human

Target Name

DAPK2

Target Full Name

Death-associated protein kinase 2

Target Function

Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell death signals, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Acts as a mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation. Regulates granulocytic motility by controlling cell spreading and polarization.; Isoform 2 is not regulated by calmodulin. It can phosphorylate MYL9. It can induce membrane blebbing and autophagic cell death.

Target Subcellular Location

Cytoplasm. Cytoplasmic vesicle, autophagosome lumen.

Target Protein Families

Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily

Target Tissue Specificity

Expressed in neutrophils and eosinophils. Isoform 2 is expressed in embryonic stem cells (at protein level). Isoform 1 is ubiquitously expressed in all tissue types examined with high levels in heart, lung and skeletal muscle.

Target Synonyms

DAK2; DAP kinase 2; DAP kinase related protein 1; DAP kinase related protein 1 beta isoform; DAP-kinase-related protein 1; DAPK2; DAPK2_HUMAN; Death associated protein kinase 2; Death-associated protein kinase 2; DRP 1; DRP-1; DRP1; MGC119312

Target Background

This gene encodes a protein that belongs to the serine/threonine protein kinase family. This protein contains a N-terminal protein kinase domain followed by a conserved calmodulin-binding domain with significant similarity to that of death-associated protein kinase 1 (DAPK1), a positive regulator of programmed cell death. Overexpression of this gene was shown to induce cell apoptosis. It uses multiple polyadenylation sites.