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P3862

Sigma-Aldrich

Anti-phospho-PKB (pThr308) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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Synonym(s):
Anti-phospho-Akt
MDL number:
NACRES:
NA.44

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 56 kDa

species reactivity

rat, mouse

technique(s)

microarray: suitable
western blot: 1:1,000 using a whole extract of PDGF-treated mouse fibroblast NIH3T3 cells and a whole extract of H2O2-treated rat fibroblast Rat-1 cells

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

phosphorylation (pThr308)

Gene Information

human ... AKT1(207)
mouse ... Akt1(11651)
rat ... Akt1(24185)

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This Item
P0244S6311SAB4200753
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

-

antibody form

IgG fraction of antiserum

antibody form

IgG fraction of antiserum

antibody form

affinity isolated antibody

antibody form

purified from hybridoma cell culture

clone

polyclonal

clone

polyclonal

clone

polyclonal

clone

AK-11, monoclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous glycerol solution

form

buffered aqueous solution

mol wt

antigen 56 kDa

mol wt

antigen 68 kDa

mol wt

-

mol wt

~56 kDa

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General description

Protein kinase B (PKB, also known as Akt) is a serine/threonine protein kinase and a key regulator of signal transduction processes. Important processes such as cell cycle, proliferation and apoptosis are regulated by PKB in response to stimuli such as growth factors, insulin and cytokines. Three isoforms of PKB have been identified, α, β and γ. PKB α is reportedly overexpressed in breast cancer cell lines, whereas PKB β is overexpressed in ovarian and pancreatic cancers. On cell stimulation by growth factors or insulin, PKB α translocates to the cell membrane, where it undergoes full activation by phosphorylation at Thr308 and Ser 473, by PDK1 and PDK2. PKB α plays a crucial role in several downstream pathways involved in glycogen synthesis, protein translation and cell proliferation. PKB is also a potent inhibitor of apoptotic cell death by suppressing BAD-induced death
Anti-phospho PKB (pThr308) recognises PKB phosphorylated at threonine 308 (56 kDa).

Immunogen

synthetic phosphopeptide corresponding to the pThr308 region of human PKBα (amino acids 301-315).

Application

Anti-phospho PKB (pThr308) may be used for detection and localization of phospho-PKB by immunoblotting. A minimum dilution of 1:1000 may be used for detection by immunoblotting in PDGF-treated mouse NIH3T3 cells and peroxide-treated Rat-1 fibroblast cell line.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM 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.

Storage Class Code

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Cellular survival: a play in three Akts.
S R Datta et al.
Genes & development, 13(22), 2905-2927 (1999-12-02)
M A Lawlor et al.
Journal of cell science, 114(Pt 16), 2903-2910 (2001-11-01)
The serine/threonine protein kinase PKB (also known as Akt) is thought to be a key mediator of signal transduction processes. The identification of PKB substrates and the role PKB phosphorylation plays in regulating these molecules have been a major focus
D R Alessi et al.
Current biology : CB, 7(4), 261-269 (1997-04-01)
Protein kinase B (PKB), also known as c-Akt, is activated rapidly when mammalian cells are stimulated with insulin and growth factors, and much of the current interest in this enzyme stems from the observation that it lies 'downstream' of phosphoinositide

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