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OP74

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Anti-PKC (Ab-2) Mouse mAb (MC5)

Synonym(s):

Anti-Protein Kinase C

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About This Item

antibody form

purified antibody

clone

MC5, monoclonal

form

liquid

contains

≤0.1% sodium azide as preservative

species reactivity

mouse, bovine, rat, human

isotype

IgG2a

General description

Purified mouse monoclonal antibody generated by immunizing BALB/c mice with the specified immunogen and fusing splenocytes with X-63 mouse myeloma cells. Recognizes ~79-80 kDa α, β1, and β2 isoforms of protein kinase C.
Recognizes the ~79-80 kDa protein kinase C α/β1/β2 isoforms in NIH3T3 cells and brain tissue.
The protein kinase C (PKC) family of protein consists of 12 known isozyme members which are classified as Ca++/phosphatidylserine-dependent, serine/threonine kinases. In addition to their involvement in signal transduction they are also involved with cell proliferation, differentiation and function. PKCγ is found primarily in the brain and spinal cord. Expression in other tissues including epidermal, adrenal, haematopoietic, and some tumors is low or variable.
This Anti-PKC (Ab-2) Mouse mAb (MC5) is validated for use in Blocking Studies, Immunoblotting, Immunoprecipitation, Paraffin Sections for the detection of PKC (Ab-2).

Immunogen

Epitope: within the hinge region of PKC
purified bovine brain PKC

Application

Blocking Studies (5 μg/ml, see comments)
Immunoblotting (1 μg/ml)
Immunoprecipitation (see application references)
Paraffin Sections (5 μg/ml, no pre-treatment required)

Physical form

In 50 mM sodium phosphate buffer, 0.2% gelatin.

Analysis Note

Positive Control
NIH3T3 cells or brain tissue

Other Notes

May be used to block the down regulation of PKC activity. Antibody should be titrated for optimal results in individual systems.

Certificates of Analysis (COA)

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Studies and prospectives of the protein kinase c family for cellular regulation.
Y Nishizuka
Cancer, 63(10), 1892-1903 (1989-05-15)
H Xiao et al.
Journal of neurosurgery, 81(5), 734-740 (1994-11-01)
Levels of protein kinase C (PKC) isoforms in eight human glioblastoma cell lines and two normal human glial cell cultures were determined. Earlier studies identified PKC-alpha and PKC-gamma in these cell lines but PKC-beta was not present. In this study
W C Wetsel et al.
The Journal of cell biology, 117(1), 121-133 (1992-04-01)
Polyclonal isoenzyme-specific antisera were developed against four calcium-independent protein kinase C (PKC) isoenzymes (delta, epsilon, epsilon', and zeta) as well as the calcium-dependent isoforms (alpha, beta I, beta II, and gamma). These antisera showed high specificities, high titers, and high
N Hirabayashi et al.
Molecular carcinogenesis, 3(3), 171-180 (1990-01-01)
The present study has characterized several aspects of the mouse epidermal protein kinase C (PKC) system and compared phorbol ester-sensitive and -resistant mice. Protein immunoblots of partially purified epidermal PKC preparations from SENCAR and C57BL/6 mice indicated the presence of
L Jin et al.
The American journal of pathology, 142(2), 569-578 (1993-02-01)
Protein kinase C (PKC) is involved in the differentiation and growth regulation of a variety of tissues including anterior pituitary gland cells. To determine the distribution of PKC in different types of adenomas, PKC activity was analyzed in human pituitary

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