Rabbit anti-Human DCLK1 Polyclonal Antibody

Uniprot Id

O15075

Target Species

Human

Target Name

DCLK1

Target Full Name

Serine/threonine-protein kinase DCLK1

Target Function

Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system.

Target Protein Families

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

Target Tissue Specificity

In fetal tissues, highly expressed in brain, detectable in lung and liver, but not in kidney. In adult tissues, expressed ubiquitously in the brain, detectable in the heart, liver, spleen, thymus, prostate, testis, ovary, small intestine and colon. The ty

Target Synonyms

Calcium/calmodulin-dependent protein kinase type I-like CPG16; CL1; CLICK1; Cpg16; DCDC3A; Dcl; Dclk; Dclk1; DCLK1_HUMAN; Doublecortin domain-containing protein 3A; Doublecortin-like and CAM kinase-like 1; Doublecortin-like kinase 1; KIAA0369; Serine/threonine-protein kinase DCAMKL1; Serine/threonine-protein kinase DCLK1

Target Background

This gene encodes a member of the protein kinase superfamily and the doublecortin family. The protein encoded by this gene contains two N-terminal doublecortin domains, which bind microtubules and regulate microtubule polymerization, a C-terminal serine/threonine protein kinase domain, which shows substantial homology to Ca2+/calmodulin-dependent protein kinase, and a serine/proline-rich domain in between the doublecortin and the protein kinase domains, which mediates multiple protein-protein interactions. The microtubule-polymerizing activity of the encoded protein is independent of its protein kinase activity. The encoded protein is involved in several different cellular processes, including neuronal migration, retrograde transport, neuronal apoptosis and neurogenesis. This gene is up-regulated by brain-derived neurotrophic factor and associated with memory and general cognitive abilities. Multiple transcript variants generated by two alternative promoter usage and alternative splicing have been reported, but the full-length nature and biological validity of some variants have not been defined. These variants encode different isoforms, which are differentially expressed and have different kinase activities.