Anti-BRSK1 / Brain-selective kinase 1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. BR serine/threonine kinase 1 is an enzyme that in humans is encoded by the BRSK1 gene. BRSK1 was initially identified as a mammalian homolog to the fission yeast S. pombe Cdr2, a mitosis-regulatory kinase and also shows significant homology to the C. elegans neuronal cell polarity regulator SAD1. BRSK1 is unbiquitously expressed, with highest levels of expression in the brain and testes. Similar to its yeast homolog, BRSK1 is thought to be involved in stress-induced cell cycle arrest. Overexpression of this protein leads to the G2/M arrest in HeLa S2 cells and UV-induced G2/M arrest could be partially abrogated by reduced expression of BRSK1 through the use of siRNA, indicating its role in DNA damage checkpoint function. More recently, it has been shown that both BRSK1 and the related protein BRSK2 are required for mammalian neuronal polarization. While BRSK1- and BRSK2-null mice were viable, double-mutant mice died within two hours of birth. Neurons from these mice showed uniformly-sized neurites as opposed to the normal long axon and multiple shorter dendrites. These neurites also displayed both axonal and dendritic markers. At least two isoforms of BRSK1 are known to exist. Protein function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C. [The UniProt Consortium]