Protein Kinase C Inhibitor, zeta, Pseudosubstrate, Myristoylated, Highly Purified

Protein Kinase C Inhibitor, zeta, Pseudosubstrate, Myristoylated, Highly Purified
Item number Size Datasheet Manual SDS Delivery time Quantity Price
P9103-71.1 1 mg - -

3 - 19 business days*

280.00€
 
Activation of PKC is one of the earliest events in the cascade leading to a variety of cellular... more
Product information "Protein Kinase C Inhibitor, zeta, Pseudosubstrate, Myristoylated, Highly Purified"
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. P9103-71 is a cell permeable protein kinase C (PKC) zeta inhibitor. , Sequence (linear): Myr-Ser-Ile-Tyr-Arg-Arg-Gly-Ala-Arg-Arg-Trp-Arg-Lys-Leu-OH, Amino Acid Analysis: Confirms expected sequence , Peptide Content: ~80.0 ± 4%, , Solubility: Soluble in distilled water at 1mg/ml. Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Stable for 12 months at -20°C. Reconstitute to nominal volume (see reconstitution instructions for peptides) and store at -20°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.
Supplier: United States Biological
Supplier-Nr: P9103-71

Properties

Conjugate: No
MW: 1928.00 D
Format: Highly Purified

Database Information

Handling & Safety

Storage: -20°C
Shipping: +4°C (International: +4°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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