MARK1 Protein, Human

MARK1 is an important serine/threonine protein kinase that critically regulates cell polarity and microtubule dynamics. It phosphorylates microtubule-associated proteins (DCX, MAP2, MAP4, MAPT/TAU), causing their dissociation and disassembly. MARK1 Protein, Human is the recombinant human-derived MARK1 protein, expressed by E. coli , with tag free. The total length of MARK1 Protein, Human is 751 a.a., .

MARK1, a serine/threonine-protein kinase, plays a crucial role in cellular processes, particularly in the regulation of cell polarity and microtubule dynamics. It achieves this by phosphorylating microtubule-associated proteins such as DCX, MAP2, MAP4, and MAPT/TAU, causing their detachment from microtubules and subsequent disassembly. In the context of neuronal migration, MARK1's dual activities in regulating cellular polarity and microtubule dynamics, potentially through the phosphorylation and regulation of DCX, contribute to its involvement in this process. Furthermore, MARK1 acts as a positive regulator of the Wnt signaling pathway, likely by mediating the phosphorylation of disheveled proteins (DVL1, DVL2, and/or DVL3), adding another layer to its multifaceted role in cellular regulation.

Human

E. coli

Tag Free

Q9P0L2 (N45-L795)

4139

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.