P9103-59A

Rabbit Anti-Protein Kinase C, mu (PKCu)

Protein kinase C ('PKC', EC 2.7.11.13) is a cyclic, nucleotide-independent enzyme that phosphorylates serine and threonine residues. The PKC family is divided into three groups depending on each the enzymes' cofactor requirements: conventional (c)PKC isoforms (α, βI, βII, and γ) require diacylglycerol (DAG), Ca2+, and phospholipids for activation; novel (n)PKC isoforms (δ, ε, η (also known as PKC-L), θ, and µ the mouse homolog of human PKCµ (also known as PKD)) require DAG but not Ca2+ for activation; and atypical (a)PKC isoforms, (ζ, ι, and λ, the mouse homolog of human PKC ι) require neither Ca2+ nor DAG. A new PKC member has recently been discovered and is referred to as PKCν. PKC's phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. These kinases also serve as major receptors for phorbol esters, a class of tumor promoters. Every member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. PKCμ, also known as nPKC-D1 and nPKC-mu, is a member of PKC family of serine/threonine kinases. PKCμ has two characteristic cysteine-rich repeats, a conserved ATP-binding consensus sequence in the kinase domain, and the invariate aspartate essential for kinase activity.