Protein Kinase C, beta (PRKCB) (AA 126-324) antibody

Antigen: Protein Kinase C, beta (PRKCB)

Synonyms: PKCB, PRKCB1, PRKCB2, MGC41878, PKC-beta, Pkcb, Prkcb1, Prkcb2, PKC-Beta, A130082F03Rik, Prkcb, MGC63591, zgc:63591, PRKCB

Binding Site: AA 126-324

Clonality: Monoclonal (36)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP)

Catalog no.: ABIN967768

Additional Information

Alternative name: PKC beta

Immunogen: Human PKCbeta

Cross-Reactivity: Rat (Rattus), Mouse (Murine), Chicken

Format: Liquid

Isotype: IgG2b

Clone: 36

Description: 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. These proteins are products of multiple genes and alternative splicing. PKC consists of a single polypeptide chain containing four conserved regions (C) and five variable regions (V). The N-terminal half containing C1, C2, V1, and V2 constitutes the regulatory domain and interacts with the PKC activators Ca2+, phospholipid, diacylglycerol, or phorbol ester. However, the novel PKC (nPKC) subfamily members ( delta, epsilon, eta, and theta isoforms) and the atypical PKC (aPKC) subfamily members (zeta, iota, and lambda isoforms) are Ca2+ independent and lack the C2 domain. The aPKC members are unique in that their activity is independent of diacylglycerols and phorbol esters. They also lack one repeat of the cysteine-rich sequences that are conserved in cPKC and nPKC. The C-terminal region of PKC contains the catalytic domain. The PKC pathway represents a major signal transduction system that is activated following ligand-stimulation of transmembrane receptors by hormones, neurotransmitters and growth factors. PKCbeta is highly expressed in brain and hematopoietic cells. Autophosphorylation of PKCbeta occurs at the N- and C-terminal regions, as well as within the hinge region. However, only the COOH- terminal autophosphorylation sites are essential for PKCbeta's function and subcellular localization. PKCbeta is critical for the proliferation of K562 cells, as well as being an important regulator of human melanogenesis.

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
4. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.

Molecular Weight: 80kDa

Comments:

Related Products: ABIN968545, ABIN967389

Application Details

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20° C.

Restrictions: For Research Use only

Images

Western blot analysis of PKCß on rat brain lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of anti-PKCß antibody.

Publications

Product: Bell, Burns: "Lipid activation of protein kinase C." in: The Journal of biological chemistry, Vol. 266, Issue 8, pp. 4661-4, 1991 (PubMed).

Soderling: "Protein kinases. Regulation by autoinhibitory domains." in: The Journal of biological chemistry, Vol. 265, Issue 4, pp. 1823-6, 1990 (PubMed).

Nishizuka: "The molecular heterogeneity of protein kinase C and its implications for cellular regulation." in: Nature, Vol. 334, Issue 6184, pp. 661-5, 1988 (PubMed).

Stebbins, Mochly-Rosen: "Binding specificity for RACK1 resides in the V5 region of beta II protein kinase C." in: The Journal of biological chemistry, Vol. 276, Issue 32, pp. 29644-50, 2001 (PubMed).

Masur, Lang, Niggemann et al.: "High PKC alpha and low E-cadherin expression contribute to high migratory activity of colon carcinoma cells." in: Molecular biology of the cell, Vol. 12, Issue 7, pp. 1973-82, 2001 (PubMed).