PKC alpha (PRKCA) antibody RabMAb®

Cat.#: 1510-1
Abcam ID: ab32376

Rabbit Monoclonal Antibody

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Description

Activation of PKC plays a crucial role in tranducing signals for a variety of cellular responses, including tumor proliferation (1). PKC isoforms have been classified into three groups: classical, novel, and atypical. Members of these three PKC groups contain an autoinhibitory domain that binds to the substrate binding site in the catalytic domain, preventing its activation in the absence of cofactors or activators (2,3). The activity of PKC is under the control of three distinct phosphorylation events, including that of the Thr641 autophosphorylation site (4).

Recommended Applications

WB, IHC, ICC, IP, FC

Applications and Recommended Dilution Factors

WB: 1:1,000-10,000
IHC: 1:250-500
ICC: 1:250-500
IP: 1:100
FC: 1:100

Species Reactivity *

Human, Mouse, Rat

*Cross reactivity determined by western blot only.

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Products Data

A. Western blot analysis on 293 cell lysate using anti-PKC alpha RabMAb (cat. # 1510-1).	B. Immunohistochemical analysis of paraffin-embedded human lung carcinoma using anti-PKC alpha RabMAb (cat. #1510-1).	C. Immunofluorescent staining of HeLa cells using anti-PKC alpha RabMAb (cat. #1510-1).

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Specificity

A synthetic peptide corresponding to residues in C-terminus of human PKCa was used as immunogen.

Storage Condition and Buffer

Store at -20 °C. Buffer: Antibody buffer, sodium azide, glycerol, and BSA. Stable for 12 months from date of receipt.

Alternative Names

PRKCA antibody, AAG6 antibody, PKC-alpha antibody, PKCA antibody, PRKACA antibody, Protein kinase C alpha type antibody

Description References

1. J Nishizuka, Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308: 693
2. Newton, A.C. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270: 28495
3. Mellor, H. and P. Perker. The extended protein kinase C superfamily. Biochem. J. 332: 281
4. Keranen, L., et al. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr. Biol. 5: 1394

Product References

1. Pysz MA, Leontieva OV, Bateman NW, et al, PKCα tumor suppression in the intestine is associated with transcriptional and translational inhibition of cyclin D1 ,Exp Cell Res 315 (2009) 1415-1428
[Application: WB, IHC]

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