Kinase Domain of Pyruvate Kinase, porcine liver

The Kinase Domain of Pyruvate Kinase, Porcine Liver is a purified, functionally active protein fragment representing the catalytic core of the Pyruvate Kinase M1/M2 isoforms (PKM2) derived from porcine liver tissue. This domain retains the enzyme's critical ability to transfer a phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP), generating pyruvate and adenosine triphosphate (ATP)—the final and rate-limiting step of glycolysis.

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TECHNICAL SPECIFICATIONS

Item	Specification
Product Name	Kinase Domain of Pyruvate Kinase, porcine liver
CAS NO.	/
Appearance	White to off-white lyophilized powder
Molecular Formula	C32H62N12O13P
Molecular Weight	853.88g/mol
Purity (RP-HPLC)	≥90%
Solubility	Soluble in water (≥ 5 mg/mL), dilute acetic acid, or DMSO; also soluble in phosphate-buffered saline (PBS)
Endotoxin	≤0.5 EU/μg
Biological Activity	Retains kinase catalytic activity, measured by phosphate transfer to ADP using phosphoenolpyruvate as substrate; specific activity ≥ 50 U/mg
Storage Conditions	Store at -80°C for long-term stability; stable for 6 months at -20°C.
Stock Location	Stock in USA
MOQ	1g

1.MECHANISM OF ACTION

This protein domain functions as a phosphotransferase enzyme, specifically catalyzing the final ATP-generating step of glycolysis. Its catalytic mechanism involves a concerted, bi-bi ordered reaction. The enzyme binds phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP) in its active site, facilitating the direct transfer of the high-energy phosphoryl group from PEP to ADP. This reaction produces one molecule of pyruvate and one molecule of ATP.

2.PRODUCT INDICATIONS

Enzyme Kinetics & Allosteric Regulation Studies: Characterizing substrate affinity (Km for PEP/ADP), catalytic rate (kcat), and the effects of allosteric activators (e.g., FBP) or inhibitors (e.g., ATP, phenylalanine) on the isolated catalytic domain.
Cancer Metabolism Research: Investigating the role of PKM2 regulation in the Warburg effect, using the porcine domain as a model due to its high homology and similar regulatory properties to human PKM2.
Drug Discovery & Screening: Serving as the direct target in high-throughput screening (HTS) campaigns to identify novel small-molecule activators or inhibitors of PKM2 for potential applications in cancer or metabolic diseases.
Structural Biology: Providing a simplified, stable protein construct for X-ray crystallography or cryo-electron microscopy studies to determine atomic-level structures in complex with substrates, allosteric effectors, or drug candidates.
Comparative Biochemistry: Studying evolutionary conservation of pyruvate kinase structure-function relationships across species.

3.CLINICAL EFFICACY OF PRODUCT

Research Tool Efficacy: Its efficacy is defined by its ability to provide consistent, high-quality enzymatic activity for mechanistic studies and compound screening, generating reliable data that informs downstream development.
Therapeutic Target Validation: PKM2, and specifically its dysregulated activity, is a well-validated target in oncology. Tumor cells often express the PKM2 isoform, which can be manipulated to favor a glycolytic phenotype that supports rapid growth.
Drug Development Context: Research using this and similar purified PKM2 constructs has fueled the discovery of PKM2 modulators. Small-molecule activators (e.g., TEPP-46, DASA-58) that promote the active tetrameric form have shown promise in preclinical models by reversing the Warburg effect and inhibiting tumor growth. These compounds were identified and characterized using isolated PKM2 protein.
Clinical Status: While no PKM2-targeted drug has yet received FDA approval, several candidates have progressed to early-phase clinical trials. This purified domain plays a foundational role in the preclinical research pipeline that validates the target and identifies lead compounds.

4.DELIVERY & SHIPPING

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Main Method: International Air Freight

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