A phospho specific peptide corresponding to residues surrounding Threonine 215 of human MARK1 was used as an immunogen. This antibody only detects MARK1 phosphorylated at Threonine 215.
Buffer
Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.
MARK belongs to the AMPK (adenosine-monophosphate activated protein kinase) branch of the CAMK (calcium/calmodulin-dependent protein kinase) group of kinases (1). MARK1 has an important neuronal function, like other MARK proteins (2). It phosphorylates Tau and related microtubule-associated proteins (MAPs) at specific sites in the microtubule binding repeats. Phosphorylation of Tau by MARK1 results in the detachment from microtubules and affects microtubule dynamics and microtubule-based intracellular transport (3). MARK1 is activated by phosphorylation on Threonine 215 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39 (4). Moreover, hyperphosphorylation by MARK1 is implicated in the initial step for the abnormal aggregation of Tau in Alzheimer’s disease (3).
Related Pathway
Adherens junction
Delta-Notch Signaling Pathway
EGFR1 Signaling Pathway
Focal Adhesion
MAPK signaling pathway
Melanogenesis
Senescence and Autophagy
TGF Beta Signaling Pathway
Toll-like receptor signaling pathway
Wnt Signaling Pathway
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Western blot analysis on SH-SY5Y cell lysates using anti-Phospho-MARK1 (pT215) RabMAb. Cells were either (A) untreated or (B) treated with Okadaic acid and Calyculin A.
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