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Key Documents

P8371

Sigma-Aldrich

Anti-Protein Kinase Cβ2 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-PKCβ2

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About This Item

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

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, mouse, rat

technique(s)

western blot: 2 μg/mL using recombinant human PKC beta II

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PRKCB(5579)
mouse ... Prkcb(18751)
rat ... Prkcb(25023)

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 recognises PKC β2 (80 kDa).

Immunogen

synthetic peptide corresponding to amino acid residues 654-665 from human PKCβ2.

Application

Anti-Protein Kinase C β2 antibody may be used for detection by immunoblotting at a working concentration of 2μg/mL.

Physical form

Solution in phosphate buffered saline containing 1.0 mg/mL BSA and 0.05% sodium azide.

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

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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Domain interactions in protein kinase C.
C J Pears et al.
Journal of cell science, 100 ( Pt 4), 683-686 (1991-12-01)
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
Alexandra C Newton
The Biochemical journal, 370(Pt 2), 361-371 (2002-12-24)
Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic
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
Susan F Steinberg
Physiological reviews, 88(4), 1341-1378 (2008-10-17)
Protein kinase C (PKC) isoforms comprise a family of lipid-activated enzymes that have been implicated in a wide range of cellular functions. PKCs are modular enzymes comprised of a regulatory domain (that contains the membrane-targeting motifs that respond to lipid

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