Abcam, ab181693, Biotin Anti-PKM antibody

Size: 100µg
Goat Polyclonal KPYM antibody - conjugated to Biotin. Suitable for ELISA, WB and reacts with Rabbit samples. Cited in 2 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human PKM.
Key facts
Host species:Goat,
Clonality:Polyclonal,
Isotype:IgG,
Conjugation:Biotin,
Carrier free:No,
Reacts with:Rabbit,
Applications:WB, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Native Full Length Protein corresponding to Human PKM.P14618,
Specificity:Anti-Pyruvate Kinase has been reported to react with all forms of pyruvate kinase (pan M-PK). Cross reactivity against Pyruvate Kinase from other sources may occur but have not been specifically determined.

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Purification technique-Ion exchange chromatography, Purification notes-Anti-Pyruvate Kinase Antibody is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer., Storage buffer-Preservative: 0.01% Sodium azideConstituents: 1% BSA, 0.88% Sodium chloride, 0.424% Potassium phosphate solution, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
PKM also known as pyruvate kinase muscle isozyme (PKM) and PEP is an enzyme that plays an important role in glycolysis by catalysing the conversion of phosphoenolpyruvate (PEP) to pyruvate yielding ATP in the process. The PKM protein has two isoforms PKM1 and PKM2 which result from alternative splicing of the PKM gene. The mass of PKM2 the more studied isoform is approximately 58 kDa. PKM is expressed in various tissues prominently in skeletal muscle heart brain and many tumor cells. Additionally PKM has significant activity in rapidly proliferating cells suggesting its importance in high-energy demanding environments.
Biological function summary
PKM functions not only in catalyzing the last step of glycolysis but also regulates metabolic and transcriptional processes. Specifically PKM2 is a participant in the regulation of gene expression and cellular response to oxidative stress and nutrient availability. It can exist as a dimer or tetramer with the latter being the more active form in glycolytic pathways while the dimeric form can translocate to the nucleus to perform functions unrelated to its glycolytic activity. These transformations make PKM part of a dynamic complex that responds to various cellular signals.
Pathways
PKM integrates into essential metabolic pathways including the glycolytic pathway and influences the pentose phosphate pathway. It works in conjunction with phosphofructokinase-1 (PFK1) another key glycolytic enzyme synchronizing the energy production process in cells. PKM2's non-metabolic roles involve interactions in signaling pathways related to cellular proliferation and survival often interacting with and modulating proteins like HIF-1α which plays a central role in cellular responses to hypoxia.
PKM2 shows strong connections to cancer and metabolic diseases. Tumor cells often exhibit a shift in expression from PKM1 to PKM2 facilitating the altered metabolism known as the Warburg effect characterized by increased aerobic glycolysis. Its interaction with HIF-1α promotes adaptation to low oxygen environments typical in tumorous growth. Furthermore PKM disruptions or aberrations contribute to metabolic disorders such as diabetes where altered glucose metabolism becomes evident. The protein's behavior in these disease conditions indicates potential targets for therapeutic intervention highlighting the importance of PKM in both normal physiology and pathology.