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Anti-PPM1K Antibody

     
  • 1 - Anti-PPM1K Antibody AP53362
    Western blot analysis of PPM1K expression in A549 (A), H1792 (B), CT26 (C), PC12 (D) whole cell lysates. (Predicted band size: 40 kD; Observed band size: 36 kD)
  • 19 - Anti-PPM1K Antibody AP53362
    Immunohistochemical analysis of PPM1K staining in human breast cancer formalin fixed paraffin embedded tissue section. The section was pre-treated using heat mediated antigen retrieval with sodium citrate buffer (pH 6.0). The section was then incubated with the antibody at room temperature and detected using an HRP conjugated compact polymer system. DAB was used as the chromogen. The section was then counterstained with haematoxylin and mounted with DPX.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC
Primary Accession Q8N3J5
Reactivity Human, Mouse, Rat, Bovine
Host Rabbit
Clonality Polyclonal
Calculated MW 40997 Da
Additional Information
Gene ID 152926
Other Names PP2CM; Protein phosphatase 1K mitochondrial; PP2C domain-containing protein phosphatase 1K; PP2C-like mitochondrial protein; PP2C-type mitochondrial phosphoprotein phosphatase; PTMP; Protein phosphatase 2C isoform kappa; PP2C-kappa
Target/Specificity KLH-conjugated synthetic peptide encompassing a sequence within the center region of human PPM1K. The exact sequence is proprietary.
Dilution WB~~WB (1/500 - 1/1000)
IHC~~1:100~500
Format Liquid in 0.42% Potassium phosphate, 0.87% Sodium chloride, pH 7.3, 30% glycerol, and 0.01% sodium azide.
StorageStore at -20 °C.Stable for 12 months from date of receipt

For Research Use Only. Not For Use In Diagnostic Procedures.

Protein Information
Name PPM1K {ECO:0000303|PubMed:23086801, ECO:0000312|HGNC:HGNC:25415}
Function Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser- 455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715).
Cellular Location Mitochondrion matrix. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:A6K136}
Research Areas

REFERENCES

Lu G.,et al.Genes Dev. 21:784-796(2007).
Mao Y.,et al.Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
Joshi M.A.,et al.Biochem. Biophys. Res. Commun. 356:38-44(2007).
Xu J.,et al.Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).

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