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Rabbit Polyclonal Phospho-PDK1 (S241) antibody (STJ90382)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, IHC, ELISA
Recommended dilution: WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:20000;
Recommended protocols: check protocols
Click or hover above images to see image description for PDK1 (phospho Ser241) Polyclonal Antibody.
Check alternative names for the antibodyExpand
PDPK1 antibody, PDK1 antibody,|3 phosphoinositide dependent protein kinase 1 antibody|3-phosphoinositide-dependent protein kinase 1 antibody|hPDK 1 antibody|hPDK1 antibody|MGC20087 antibody|MGC35290 antibody|OTTHUMP00000159109 antibody|OTTHUMP00000159110 antibody|OTTHUMP00000174525 antibody|PDK1 antibody|Pdpk1 antibody|PDPK1_HUMAN antibody|PDPK2 antibody|PDPK2P antibody|PkB kinase antibody|PkB kinase like gene 1 antibody|PkB like 1 antibody|PRO0461 antibody|Protein kinase antibody|Anti-PDPK1 antibody [EP569Y] (ab52893)
SCBT cat No: sc-136243|sc-17766|sc-7686|sc-376586|sc-17765|sc-9118|sc-398815|sc-133901|
PDK1 (phospho Ser241) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Phospho-PDK1 (S241) Polyclonal Antibody detects endogenous levels of PDK1 protein only when phosphorylated at S241.
Synthesized phospho-peptide derived from PDK1 (phospho Ser241) at AA range 180-260
WB, IHC, ELISA
|Recommended dilution|| |
WB 1:500-1:2000; IHC 1:100-1:300; ELISA 1:20000;
|Molecular weight|| |
PDK1 (phospho Ser241) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
PDK1 (phospho Ser241) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
3-phosphoinositide-dependent protein kinase 1 antibody, hPDK1 antibody,
|Protein names|| |
3-phosphoinositide-dependent protein kinase 1 , hPDK1 ,
|Protein function|| |
Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca2+ entry and Ca2+-activated K+ channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive. / ATP + a protein = ADP + a phosphoprotein. / Homodimerization regulates its activity by maintaining the kinase in an autoinhibitory conformation. NPRL2 down-regulates its activity by interfering with tyrosine phosphorylation at the Tyr-9, Tyr-373 and Tyr-376 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-241 residue. STRAP positively regulates its activity by enhancing its autophosphorylation and by stimulating its dissociation from YWHAQ. SMAD2, SMAD3, SMAD4 and SMAD7 also positively regulate its activity by stimulating its dissociation from YWHAQ. Activated by phosphorylation on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin.
|Protein tissue specificity|| |
Appears to be expressed ubiquitously. The Tyr-9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast.
|Protein sequence and domain|| |
The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization. / The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors. / Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDPK1 subfamily. / Contains 1 PH domain. / Contains 1 protein kinase domain.
|Protein post-translational modifications|| |
Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5. / Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2. / Monoubiquitinated in the kinase domain, deubiquitinated by USP4.
|Protein cellular localization|| |
Cytoplasm / Nucleus / Cell membrane; Peripheral membrane protein / Cell junction > focal adhesion
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St John’s Laboratory Ltd.
|Product type|| |
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