Recombinant Human Pyruvate kinase PKM (PKM), partial

Overview

Recombinant Human Pyruvate kinase PKM (PKM), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Cancer research by enabling enzyme activity assays, kinetics/structure–function studies and inhibitor or substrate screening in controlled in vitro settings.

Key elements and design rationale

• Expressed region: 185-461aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
• Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
• Tag / fusion: N-terminal GST-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
• Molecular weight (reported): 57.4 kDa. Apparent size may vary with tags, processing, and gel conditions.

When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.

Biological background

The gene commonly associated with this target is PKM. PKM refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.

Research relevance and current trends

• Mapping pathway dependencies and signaling networks that drive tumor growth and drug resistance.
• Developing and benchmarking biomarker assays (e.g., immunoassays or binding reagents) for candidate targets.
• Characterizing protein variants, domains, or interaction partners relevant to targeted therapeutics and precision oncology.

Relevance: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. 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.; [Isoform M2]: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity. In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase. Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase. Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription. Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis. Promotes the expression of the immune checkpoint protein CD274 in ARNTL/BMAL1-deficient macrophages. May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs. Plays a role in caspase independent cell death of tumor cells.; [Isoform M1]: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth. In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity.

Common research applications

• Enzyme activity assays and kinetics measurements with defined substrates/cofactors.
• Inhibitor, activator, or substrate screening in biochemical assay formats.
• Structure–function analysis to interpret how sequence changes impact catalytic performance.

In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.

Notes for experimental interpretation

• Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
• Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
• Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
• E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.

• Datasheet (12932744)
• MSDS (12932744)

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