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

Details for Product No. ABIN967769
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Synonyms PKC-B, Prkcb, prkcb1, zgc:63591, PKC-beta, PKCB, PRKCB1, PRKCB2, PKC, A130082F03Rik, PKC-Beta, Pkcb, Prkcb1, Prkcb2
AA 126-324
(42), (20), (15), (13), (11), (10), (6), (6), (4), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
(136), (68), (66), (5), (4), (3), (1), (1), (1)
(152), (12), (7), (3)
Clonality (Clone)
Monoclonal ()
(9), (8), (6), (5), (5), (5), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB), Immunoprecipitation (IP)
(158), (88), (59), (22), (22), (12), (10), (10), (6), (4), (3), (3), (2), (1), (1), (1), (1)
Pubmed 5 references available
Quantity 150 μg
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Catalog No. ABIN967769
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Immunogen Human PKCbeta
Clone L22FA2
Isotype IgG2b
Cross-Reactivity Rat (Rattus), Mouse (Murine), Chicken
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. 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.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name PKC beta
Background 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.
Molecular Weight 80 kDa

Related Products: ABIN968545, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Protein Kinase C, beta (PRKCB) (AA 126-324) antibody 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.
anti-Protein Kinase C, beta (PRKCB) (AA 126-324) antibody (2) anti-Protein Kinase C, beta (PRKCB) (AA 126-324) antibody (Image 2)
Product cited in: 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).

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).

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).

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

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

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