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P2584

Sigma-Aldrich

Monoclonal Anti-Protein Kinase Cβ2 antibody produced in mouse

clone PK-B26, ascites fluid

Synonym(s):

Anti-PKC β2

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

PK-B26, monoclonal

mol wt

antigen 80 kDa

contains

15 mM sodium azide

species reactivity

rat

technique(s)

microarray: suitable
western blot: 1:8,000 using rat brain cytosol preparation

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Protein Kinase C (PKC, 76-93 kD) is a family of Ser/Thr specific protein kinases that perform key functions in numerous signalling pathways, in biological systems, through their various isoforms. The conventional PKC isoforms (cPKC) are PKC-α, β1, β2 and γ; activated by phosphatidylserine, calcium or phorbol esters. Proteolysis of PKC in vivo is thought to be mediated by calpains I and II. Calpains cleave PKC in the V3 hinge region to produce two distinct fragments, one comprising the N-terminal regulatory domain (30 kD) and the other fragment containing the C-terminal kinase domain (50 kD) that is catalytically active. Multiple functions such as, cellular and vascular regulations, angiogenesis, cell growth, apoptosis, changes in basement membrane thickness, extracellular matrix organisation, MAPK signalling, are attributed to PKC isoforms. These varied functions implicate PKC isoforms in cardiac hypertrophies and diabetic nephropathy and cardiovascular complications.
Anti-Protein Kinase C β2 antibody specifically recognizes an epitope located within the amino acid residues 660-673 at the C-terminal variable (V5) region of PKCβ2 (80 kDa).

Specificity

The antibody shows no cross-reactivity with PKC peptides corresponding to C-terminal sequences from PKC β1 (658-671) and PKC γ (684-697) conjugated to BSA.

Immunogen

synthetic peptide corresponding to the C-terminal variable (V5) region (amino acids 660-673) of PKC β2.

Application

Anti-Protein Kinase C β2 antibody may be used for immunoblotting at a working dilution of 1:8000 using rat brain cytosolic extract. It is suitable for protein microarray.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids


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Ezra E W Cohen et al.
Cancer research, 69(1), 65-74 (2009-01-02)
Protein kinase Calpha (PKCalpha) has been implicated in cancer, but the mechanism is largely unknown. Here, we show that PKCalpha promotes head and neck squamous cell carcinoma (SCCHN) by a feed-forward network leading to cell cycle deregulation. PKCalpha inhibitors decrease
S Budhiraja et al.
Fundamental & clinical pharmacology, 22(3), 231-240 (2008-05-20)
Diabetic nephropathy (DN) has emerged as the major causative pathology in patients entering end-stage renal disease (ESRD) worldwide and it is responsible for 30-40% of all ESRD cases. Treatments for DN are centered on control of hyperglycemia and blood pressure
Domain interactions in protein kinase C.
C J Pears et al.
Journal of cell science, 100 ( Pt 4), 683-686 (1991-12-01)
Julio Cesar Batista Ferreira et al.
Journal of molecular and cellular cardiology, 51(4), 479-484 (2010-11-03)
Cardiac hypertrophy is a complex adaptive response to mechanical and neurohumoral stimuli and under continual stressor, it contributes to maladaptive responses, heart failure and death. Protein kinase C (PKC) and several other kinases play a role in the maladaptative cardiac
Pedro Geraldes et al.
Circulation research, 106(8), 1319-1331 (2010-05-01)
Both cardio- and microvascular complications adversely affect the life quality of patients with diabetes and have been the leading cause of mortality and morbidity in this population. Cardiovascular pathologies of diabetes have an effect on microvenules, arteries, and myocardium. It

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