Mouse PKC q Monoclonal Antibody

PKC-theta (N-terminal region)

Cat. Num. AAA470025

• Reactivity: Human, Rat, Mouse
• Applications: ELISA, Western Blot
• Purity: Protein A Purified
• Synonyms: PKC q; Monoclonal Antibody; PKC-theta (N-terminal region); PKC q (N-terminal Region); PKC theta; anti-PKC q antibody

• Host: Mouse
• Reactivity: Human, Rat, Mouse
• Clonality: Monoclonal
• Isotype: IgG2a
• Specificity: This antibody detects a 79 kDa* protein corresponding to the molecular mass of PKCq on SDS-PAGE immunoblots of human Jurkat cell lysates.
• Purity/Purification: Protein A Purified
• Form/Format: Mouse monoclonal antibody purified with protein A chromatography is supplied in 100ml phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

• Applicable Applications for anti-PKC q antibody: ELISA, Western Blot
• Application Notes: ELISA: 1:2000; Western Blot: 1:1000
• Immunogen: Clone (M217) was generated from a recombinant mouse PKCq protein that included amino acids residues in the N-terminal region. This sequence is conserved in human and rat PKCq, and has low homology to other PKC family members.
• Preparation and Storage: Store at -20 degree C. Do not aliquot. Stable for 1 year.

Testing Data

Related Product Information for anti-PKC q antibody

The Protein Kinase C (PKC) family of homologous serine/threonine protein kinases is involved in a number of processes such as growth, differentiation, and cytokine secretion. At least eleven isozymes have been described. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half interacts with PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester, while the C-terminal half contains the catalytic domain. The conventional PKC subfamily (a, bI, bII, and g) is regulated by both Ca2+ and diacylglycerol. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters, and growth factors. The phosphorylation of multiple sites in PKCs regulates their activity.

References

• Kawakami et al. (2003) Proc. Natl. Acad. Sci. USA 100:9470-9475.
• Nishizuka, Y. (1988) Nature 334:661.