PKM Monoclonal Antibody

Code CSB-MA018072A0m
Size US$350
Image
  • Western Blot
    Positive WB detected in: Hela whole cell lysate, MCF-7 whole cell lysate, Jurkat whole cell lysate, NIH/3T3 whole cell lysate
    All lanes: PKM antibody at 1:4000
    Secondary
    Goat polyclonal to Mouse IgG at 1/10000 dilution
    Predicted band size: 58 kDa
    Observed band size: 58 KDa
    Exposure time: 1min

     

  • Western Blot
    Positive WB detected in: Mouse Heart tissue, Mouse Brain tissue, Mouse Skeletal Muscle tissue
    All lanes: PKM antibody at 1:4000
    Secondary
    Goat polyclonal to Mouse IgG at 1/10000 dilution
    Predicted band size: 58 kDa
    Observed band size: 58 KDa

  • Western Blot
    Positive WB detected in: Rat Heart tissue, Rat Spleen tissue, Rat Brain tissue
    All lanes: PKM antibody at 1:4000
    Secondary
    Goat polyclonal to Mouse IgG at 1/10000 dilution
    Predicted band size: 55-60 kDa
    Observed band size: 55-60 kDa

  • Western Blot
    Positive WB detected in: MCF-7 whole cell lysate at 40µg, 20µg, 10µg, 5µg, 2.5µg, 1.25µg, 0.625µg, 0.3125µg
    All lanes: PKM antibody at 1:4000
    Secondary
    Goat polyclonal to Mouse IgG at 1/10000 dilution
    Predicted band size: 58 kDa
    Observed band size: 58 KDa
    Exposure time: 5min

  • Western Blot
    Positive WB detected in: MCF-7 whole cell lysate
    All lanes: PKM antibody at 1:4000, 1:8000, 1:16000, 1:32000, 1:64000, 1:128000, 1:256000
    Secondary
    Goat polyclonal to Mouse IgG at 1/10000 dilution
    Predicted band size: 58 kDa
    Observed band size: 58 KDa
    Exposure time: 5min

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human tonsil tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human tonsil tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human tonsil tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human lung cancer tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human lung cancer tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human lung cancer tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • IHC image of CSB-MA018072A0m diluted at 1:400 and staining in paraffin-embedded human kidney tissue performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a biotinylated secondary antibody and visualized using an HRP conjugated SP system.

  • Immunofluorescence staining of A549 cells with CSB-MA018072A0m at 1:230, counter-stained with DAPI. The cells were blocked in 10% normal Goat Serum and then incubated with the primary antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Mouse IgG(H+L).

  • Immunofluorescence staining of Hela cells with CSB-MA018072A0m at 1:230, counter-stained with DAPI. The cells were blocked in 10% normal Goat Serum and then incubated with the primary antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Mouse IgG(H+L).

  • Immunofluorescence staining of HepG2 cells with CSB-MA018072A0m at 1:230, counter-stained with DAPI. The cells were blocked in 10% normal Goat Serum and then incubated with the primary antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Mouse IgG(H+L).

  • Immunoprecipitating PKM in Hela whole cell lysate
    Lane 1: Mouse control IgG instead of CSB-MA018072A0m in Hela whole cell lysate.
    Lane 2: CSB-MA018072A0m (1?l) + Hela whole cell lysate (500?g)
    Lane 3: Hela whole cell lysate (10?g)
    For western blotting, the blot was detected with CSB-MA018072A0m at 1:2000, and a HRP-conjugated Protein G antibody was used as the secondary antibody at 1:2000

  • Overlay histogram showing Hela cells stained with CSB-MA018072A0m (red line) at 1:100. The cells were incubated in 1x PBS /10% normal goat serum to block non-specific protein-protein interactions followed by primary antibody for 1 h at 4°C. The secondary antibody used was FITC goat anti-mouse IgG(H+L) at 1/200 dilution for 1 h at 4°C. Isotype control antibody (green line) was used under the same conditions. Acquisition of >10,000 events was performed.

  • Overlay histogram showing HepG2 cells stained with CSB-MA018072A0m (red line) at 1:100. The cells were incubated in 1x PBS /10% normal goat serum to block non-specific protein-protein interactions followed by primary antibody for 1 h at 4°C. The secondary antibody used was FITC goat anti-mouse IgG(H+L) at 1/200 dilution for 1 h at 4°C. Isotype control antibody (green line) was used under the same conditions. Acquisition of >10,000 events was performed.

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Product Details

Full Product Name Mouse anti-Homo sapiens (Human) PKM Monoclonal antibody
Uniprot No. P14618
Target Names PKM
Alternative Names CTHBP antibody; Cytosolic thyroid hormone-binding protein antibody; KPYM_HUMAN antibody; OIP-3 antibody; Opa-interacting protein 3 antibody; p58 antibody; pkm antibody; PKM1 antibody; PKM2 antibody; Pyruvate kinase 2/3 antibody; Pyruvate kinase muscle isozyme antibody; Pyruvate kinase PKM antibody; THBP1 antibody; Thyroid hormone-binding protein 1 antibody; Tumor M2-PK antibody
Raised in Mouse
Species Reactivity Human, Rat, Mouse, Rabbit
Immunogen Recombinant Human Pyruvate kinase PKM protein (2-531AA)
Immunogen Species Homo sapiens (Human)
Conjugate Non-conjugated
Clonality Monoclonal
Isotype IgG1
Clone No. 6C3C7
Purification Method >95%, Protein G purified
Concentration It differs from different batches. Please contact us to confirm it.
Buffer Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form Liquid
Tested Applications ELISA, WB, IHC, IF, FC, IP
Recommended Dilution
Application Recommended Dilution
WB 1:4000-1:256000
IHC 1:200-1:500
IF 1:150-1:300
FC 1:50-1:200
IP 1µl-4µl
Protocols ELISA Protocol
Western Blotting(WB) Protocol
Immunohistochemistry (IHC) Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol
Immunoprecipitation (IP) Protocol
Troubleshooting and FAQs Antibody FAQs
Storage Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Data

Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.
Gene References into Functions
  1. results reveal that nBP1a/PKM2 interaction activates lipid metabolism genes in cancer cells and that Thr-59 phosphorylation of SREBP-1a plays an important role in cancer cell proliferation. PMID: 29514980
  2. we demonstrated that knockdown of PKM2 can inhibit GC cell proliferation, G1-S phase transition, can, especially, attenuate GC cell migration in vivo and in vitro, per contra, promote the autophagy, which may depend on mediating the PI3K-Akt signaling. PMID: 28588255
  3. PKM1 activated glucose catabolism and stimulated autophagy/mitophagy, favoring malignancy PMID: 29533781
  4. miRNA-139-5p inhibited cell proliferation, migration, and glycolysis in GBC, at least in part, by repressing pyruvate kinase M2 PMID: 30105813
  5. Mammalian target of rapamycin pathway promotes aerobic glycolysis in esophageal squamous cell carcinoma by upregulating pyruvate kinase M2 isoform PMID: 29916308
  6. PKM2 promotes tumor cell exosome release via phosphorylating protein SNAP23. PMID: 28067230
  7. proteins such as MMP2 and MMP9 as well as P38 expression were also affected by the PKM2 expression changes. These results proved that PKM2 could be involved in the progression of bladder cancer by mitogen-activated protein kinases signaling pathway. PMID: 30249877
  8. hypoxic stress in the hepatocellular carcinoma (HCC)cells promoted YAP binding to HIF-1a in the nucleus and sustained HIF-1a protein stability to bind to PKM2 gene and directly activates PKM2 transcription to accelerate glycolysis PMID: 30180863
  9. overexpressed PKM2 led to increased CCND1 and decreased CDKN1A expression, whereas underexpressed PKM2 led to decreased CCND1 and increased CDKN1A expression in ovarian cancer cells. PMID: 29752805
  10. Our current study thus unveils a distinct regulatory function of PKM2, providing new options for therapeutic intervention targeting HIV-1-host interactions. PMID: 29607934
  11. PKM2 as a novel target of RUNX1-ETO and is specifically downregulated in RUNX1-ETO positive AML patients, indicating that PKM2 level might have a diagnostic potential in RUNX1-ETO associated AML. PMID: 28092997
  12. High M2-PK expression is associated with pancreatic cancer and peri-ampullary cancer. PMID: 29540198
  13. The activity of PKM2 was indispensable for the development and metastasis of OS. PMID: 29155364
  14. fFndings demonstrate that mDC activation requires an elevated intrinsic PKM2 level and that PKM2 improves the immune status of patients with SAA by enhancing the functions of mDCs and, consequently, CTLs. PMID: 29636835
  15. EGFR activation results in c-Src-mediated Cdc25A phosphorylation at Y59, which interacts with nuclear pyruvate kinase M2 (PKM2). PMID: 27485204
  16. Study demonstrate that PKM2 plays an important role in metabolic activities, as well as in the malignancy of pancreatic ductal adenocarcinoma cells. PMID: 29393401
  17. Suggest a critical role for pyruvate kinase isozyme M2 in mediating the interaction between pancreatic cancer cells and pancreatic stellate cells. PMID: 29619774
  18. Results show that PK2 expression level is regulated by HSP90 in hepatocellular carcinoma (HCC). HSP90 enhances PKM2 stability by inducing the phosphorylation of PKM2 at Thr-328. PMID: 29262861
  19. O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect. PMID: 29229835
  20. Results indicate that PKM2 is positively correlated with Sp1 expression and demonstrate that Sp1 directly regulates its expression in castration-resistant prostate cancer. PMID: 29094170
  21. High PKM2 expression is associated with lung adenocarcinoma. PMID: 28489603
  22. Epigenetic silencing of miR-338 facilitates glioblastoma progression by preventing suppression the PKM2/beta-catenin axis. PMID: 28858851
  23. this study correlates TuM2PK with tumor size, CRP and CA 15-3 in metastatic breast carcinomas. PMID: 28869444
  24. PKM2 modulates the glycolysis and extracellular matrix generation, providing the vital role of PKM2 on osteoarthritis (OA) pathogenesis and a novel therapeutic target for OA. PMID: 29356574
  25. This work suggested that OA increased PKM1/PKM2 ratio, resulting in HNF-4alpha activation and hepatoma differentiation. PMID: 28726775
  26. the present findings enriched our knowledge by demonstrating a significant association of PKM2 and GLS1 with oxaliplatin-resistance in CRC. PMID: 28498807
  27. Elevated expression of PKM2 is a prognostic factor for poor gallbladder cancer (GBC) clinical outcomes, implied involving of PKM2 in GBC progression. PMID: 27283076
  28. PKM2 knockdown resulted in increased p53 expression and prolonged half-life of p53. PKM2 could directly bind with both p53 and MDM2 and promote MDM2-mediated p53 ubiquitination. The dimeric PKM2 significantly suppressed p53 expression compared with the other PKM2 mutants. PMID: 27801666
  29. Inhibition of the mTOR pathway abolished TGF-beta1-induced EMT and reduced mTOR/p70s6k signaling, which downregulated PKM2 expression. PMID: 28446743
  30. Study indicates that nitric oxide induces PKM2 nuclear translocation and promotes glycolysis in ovarian cancer cells. PMID: 28380434
  31. Authors report that AKT directly interacts with PKM2 and phosphorylates it at Ser-202, which is essential for the nuclear translocation of PKM2 protein under stimulation of IGF-1. In the nucleus, PKM2 binds to STAT5A and induces IGF-1-stimulated cyclin D1 expression, suggesting that PKM2 acts as an important factor inducing STAT5A activation under IGF-1 signaling. PMID: 27340866
  32. The results suggested that targeting PKM2 with an oncolytic adenovirus produced a strong antitumor effect. PMID: 28569774
  33. our results demonstrated that miR-let-7a inhibits cell proliferation, migration and invasion by down-regulation of PKM2 in cervical cancer PMID: 28415668
  34. Data show that cytomegalovirus encoded chemokine receptor US28 (US28) signaling in activation of the HIF-1alpha/PKM2 feedforward loop in fibroblasts and glioblastoma cells. PMID: 27602585
  35. High PKM2 expression is associated urothelial tumorigenesis. PMID: 26992222
  36. Report that PKM2 is succinylated at lysine 498 and succinylation increases its activity. SIRT5 binds to, desuccinylates and inhibits PKM2 activity. Increased levels of reactive oxygen species (ROS) decreases succinylation and activity of PKM2 by increasing its binding to SIRT5. PMID: 28036303
  37. over-expression of PKM2 is associated with poor prognosis in most solid cancers and it might be a potentially useful biomarker for predicting cancer prognosis in future clinical applications. PMID: 27911861
  38. Interdependence of GLO I and PKM2 in the Metabolic shift to escape apoptosis in GLO I-dependent cancer cells PMID: 29225125
  39. This study demonstrates that lapachol inhibits glycolysis in cancer cells by targeting PKM2. Unlike the previously reported inhibitor shikonin, lapachol does not target mitochondria in tumor cell growth inhibition. PMID: 29394289
  40. In this study, we indicate that P53 (N340Q/L344R) promotes hepatocarcinogenesis through upregulation of PKM2 PMID: 27167190
  41. These findings indicate that shRNA-mediated silencing of PKM2 gene promotes apoptosis and inhibits aerobic glycolysis, proliferation, migration, and invasion in colorectal cancer cells. PMID: 28543190
  42. Due to achieved results concerning expression of PKM2 there is a lack of evidence for its diagnostic and prognostic usage in ovarian cancer. PMID: 29277786
  43. UCP2 stimulates hnRNPA2/B1, GLUT1 and PKM2 expression and sensitizes pancreatic cancer cells to glycolysis inhibition. PMID: 27989750
  44. These findings uncover a novel mechanism through which mitochondrial PKM2 phosphorylates Bcl2 and inhibits apoptosis directly. PMID: 28035139
  45. These findings suggested that PKM2 and GLS might play important roles in the proliferation of hypoxic gastric cancer cells PMID: 29032577
  46. demonstrated that lincRNA-p21 blunted the prostate cancer cell proliferation and tumorigenic capacity through down-regulation of PKM2 PMID: 28994148
  47. we demonstrated that SHP-1 dephosphorylates PKM2Y105 to inhibit the Warburg effect and nucleus-dependent cell proliferation, and the dephosphorylation of PKM2Y105 by SHP-1 determines the efficacy of targeted drugs for hepatocellular carcinoma treatment PMID: 26959741
  48. The PKM2-shRNA group exhibited reduced PKM2 mRNA and protein expression, whereas p53 and p21 expression was increased compared with the blank and empty plasmid groups. PMID: 28746922
  49. The CARM1-PKM2 axis serves as a metabolic reprogramming mechanism in tumorigenesis. PMID: 29058718
  50. PKM2 activity is higher in patients with NSCLC than in healthy subjects. The level of PKM2 activity is associated with advanced stage of cancer. PMID: 27683215

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Subcellular Location Cytoplasm, Nucleus
Protein Families Pyruvate kinase family
Tissue Specificity Specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, as well as cancer cells.
Database Links

HGNC: 9021

OMIM: 179050

KEGG: hsa:5315

STRING: 9606.ENSP00000320171

UniGene: Hs.534770

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