Protein Kinase C, zeta, Substrate (PKCz) (Biotin)

Activation of PKC is one of the earliest events in the cascade leading to a variety of cellular responses such as secretion, gene expression, proliferation and muscle contraction. PKC isoforms have been classified in three groups: classical PKCs, which are Ca2+ dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG) and phorbol esters (TPA or PMA) through their cysteine-rich C1 domains; novel PKCs, which are Ca2+ independent but are still regulated by PS, DAG and TPA; and atypical PKCs, which are Ca2+ independent and do not require PS, DAG or TPA for their activation. These three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to the substrate binding site in the catalytic domain preventing its activation in the absence of cofactors or activators. Other members have been recently added to the PKC superfamily based on homology within the catalytic domain. PKCmu, or PKD, is regulated by DAG and TPA through its C1 domain. However, PKD is distinguished by a transmembrane domain and PH domain, as well as by its unique substrate recognition and Golgi localization. The PKC-related kinases, or PRKs, lack a C1 domain and thus do not respond to DAG or phorbol esters; instead they can be activated by phosphatidylinositol lipids, and their kinase activity is directly regulated by small GTPases of the Rho family through Rho binding to the homology region 1 (HR1). The activity of PKC is under control by three distinct phosphorylation events. Specifically, threonine 500 at the activation loop, the threonine 641 autophosphorylation site and the serine 660 hydrophobic site at the carboxy-terminus of PKCbeta II are phosphorylated in vivo. For the atypical PKC isoforms, there is no phosphorylation in the hydrophobic region, which has a glutamic acid residue in place of the serine or threonine residue found in other PKC isoforms. The enzyme PDK1 or perhaps a close relative is responsible for PKC activation loop phosphorylation in a phosphoinositide 3 kinase (PI3K) dependent fashion.\n\nP9103-72 is the biotinylated form of the protein kinase C (PKC) zeta substrate\n\nSequence (linear): Biot-Ser-Ile-Tyr-Arg-Arg-Gly-Ser-Arg-Arg-Trp-Arg-Lys-Leu-OH\n\nAmino Acid Analysis: Confirms expected sequence\nPeptide Content: 80.2

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SPECIFICATIONS

Catalog Number

P9103-72

Size

1mg

Conjugates

Biotin

Form

Supplied as a lyophilized powder.

Purity

~90% by HPLC and MS analysis

References

Schmitz-Peiffer, C., et al. (1998) Activated protein kinase C alpha associates with annexin VI from skeletal muscle. Biochem. J. 330:675-681.\nSajan, M. (1999) Protein Kinase C-z and Phosphoinositide-dependent Protein Kinase-1 are required for Insulin-induced Activation of ERK in Rat Adipocytes. J. Biol. Chem. 274(43):30495-30500.\nKanoh, Y., et al. (2000) Thiazolidinedione treatment enhances insulin effects on protein kinase C-z/l activation and glucose transport in adipocytes of nondiabetic and goto-kakizaki type II diabetic rats. J. Biol. Chem. 275(22):16690-16696