PKC alpha (PRKCA) Rabbit Polyclonal Antibody

CAT#: TA326807

Rabbit anti-PRKCA Polyclonal Antibody


USD 275.00

3 Weeks*

Size
    • 100 ul

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Specifications

Product Data
Applications IHC, WB
Recommended Dilution WB 1:500 - 1:2000;IHC 1:50 - 1:100
Reactivities Human, Mouse, Rat
Host Rabbit
Isotype IgG
Clonality Polyclonal
Immunogen C term -peptide of human PRKCA
Formulation Store at -20C or -80C. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3
Concentration lot specific
Purification Affinity purification
Conjugation Unconjugated
Storage Store at -20°C as received.
Stability Stable for 12 months from date of receipt.
Predicted Protein Size 77 kDa
Gene Name protein kinase C alpha
Background Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction . PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters. Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation at Thr500 in the activation loop, the autophosphorylation site at Thr641, and at carboxy-terminal hydrophobic site Ser660 occurs in vivo. Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. Either the enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCµ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization. PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity.
Synonyms AAG6; PKC-alpha; PKCA; PRKACA
Reference Data
Protein Families Druggable Genome, ES Cell Differentiation/IPS, Protein Kinase
Protein Pathways Calcium signaling pathway, ErbB signaling pathway, Fc epsilon RI signaling pathway, Fc gamma R-mediated phagocytosis, Focal adhesion, Gap junction, Glioma, GnRH signaling pathway, Leukocyte transendothelial migration, Long-term depression, Long-term potentiation, MAPK signaling pathway, Melanogenesis, Natural killer cell mediated cytotoxicity, Non-small cell lung cancer, Pathogenic Escherichia coli infection, Pathways in cancer, Phosphatidylinositol signaling system, Tight junction, Vascular smooth muscle contraction, VEGF signaling pathway, Vibrio cholerae infection, Wnt signaling pathway

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*Delivery time may vary from web posted schedule. Occasional delays may occur due to unforeseen complexities in the preparation of your product. International customers may expect an additional 1-2 weeks in shipping.