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PKA C-α (D38C6) Rabbit mAb
synthetic peptide corresponding to residues surrounding Ser326 of human PKA C-α protein
W, IP
详见说明书
CST
详见MSDS文件
大量
H,M,R,Hm,Mk
1
-20°c
100 ul (10 western blots)/carrier free & custom formulation / quantity
规格: | 产品价格: | ¥请询价 | |
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规格: | 100 ul (10 western blots) | 产品价格: | ¥请询价 |
规格: | carrier free & custom formulation / quantity | 产品价格: | ¥请询价 |
pathway more info application references datasheet PDF MSDS PDF protocols
Applications Key: W=Western Blotting IP=Immunoprecipitation
Reactivity Key: H=Human M=Mouse R=Rat Hm=Hamster Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Applications | Reactivity | Sensitivity | MW (kDa) | Isotype |
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W IP | H M R Hm Mk | Endogenous | 42 | Rabbit IgG |
Protocols | |
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Specificity / Sensitivity | PKA C-α (D38C6) Rabbit mAb recognizes endogenous levels of total PKA C-α protein. |
Source / Purification | Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser326 of human PKA C-α protein. |
Background | The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).
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Application References | Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know! |
Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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