Anti-DCLK1 is produced in rabbit using as immunogen a synthetic peptide corresponding to human DCLK1, conjugated to KLH. DCLK1 (doublecortin like kinase 1) is also known as DCLK, DCAMKL1, DCDC3A and CLICK1. DCLK1 consists of an N-terminal doublecortin (DC) domain, responsible for its localization to microtubules and a C-terminal Ser/Thr kinase domain.

DCLK1 is a neuronal transmembrane enzyme that may regulate cortical development, nerve cell migration and microtubule polymerization. This enzyme is similar to DCX, but DCLK1 additionally functions as a Ca²⁺/calmodulin-dependent protein kinase that can phosphorylate myelin basic protein and itself . Anti-DCLK1 antibody is specific for human, rat and mouse DCLK1. In immunoblotting, detection of the DCLK1 band is specifically inhibited by the DCLK1 immunizing peptide.

The corresponding sequence is highly conserved (single amino acid substitution) in rat and mouse DCLK1.

Anti-DCLK1 antibody is suitable for use in western blot (1.5-3.0 μg/mL using extracts of postnatal mouse brain (S1 fraction), postnatal rat brain (S1 fraction) and HEK-293T cells over-expressing human DCLK1). The antibody may also be used for immunoblot (approx. 81 kDa) assays.

Doublecortin-like kinase1 (DCLK1) is widely expressed in post-mitotic neurons in the developing nervous system and important for neuronal migration to cerebral cortex. DCLK1 is highly expressed during embryogenesis and is localized to neuronal growth cones where it associates with the microtubule cytoskeleton and regulates microtubule polymerization. DCLK1 kinase domain is susceptible to cleavage by the Ca²⁺ -dependent protease calpain, suggesting that a Ca²⁺ -responsive mechanism is involved in regulating the DCLK1 kinase activity during embryogenesis. DCLK1 has been identified as a putative intestinal stem cell marker.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

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