Recombinant Human PKM2 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 7244-PK

Pyruvate Kinase, Muscle
R&D Systems, part of Bio-Techne
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7244-PK-020
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Key Product Details

Source

E. coli

Accession #

P14618

Conjugate

Unconjugated

Applications

Enzyme Activity

View all PKM2 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human PKM2 protein
Ser2-Pro531, with N-terminal Met and 6-His tag

Purity

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

No sequence observed. N-terminal His tag confirmed by Western analysis.

Predicted Molecular Mass

59 kDa

SDS-PAGE

58-59 kDa, reducing conditions

Activity

Measured by its ability to transfer phosphate from phospho(enol)pyruvic acid monosodium salt hydrate (PEP) to adenosine 5'-diphosphate sodium salt (ADP).
The specific activity is >12,500 pmol/min/μg, as measured under the described conditions.

Reviewed Applications

Read 1 review rated 5 using 7244-PK in the following applications:

Formulation, Preparation and Storage

7244-PK
Formulation Supplied as a 0.2 μm filtered solution in Tris, NaCl, Glycerol, Brij-35 and DTT.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.

Background: PKM2

Pyruvate kinases are glycolytic enzymes that catalyze the transfer of a phosphoryl group from phosphoenolpyruvate to ADP, generating ATP (1), the final step in the glycolysis pathway. There are two pyruvate kinase muscle isozymes, PKM1 and PKM2, caused by alternative splicing at the carboxy termini (2). PKM2 is specifically expressed in proliferating cells, such as embryonic stem cells, embryonic carcinoma cells, and various cancer cells (3, 4). Switching from PKM1 to PKM2 in tumor cells causes the shift in cellular metabolism to aerobic glycolysis, which is important for tumor cell proliferation and survival (5). In addition, PKM2 exists in two oligomeric forms: a highly active tetrameric form and nearly inactive dimeric form (6). The ratio between the two forms determines whether glucose are channeled to biosynthetic processes or used for glycolytic ATP production. The oligomerization of PKM2 is allosterically stimulated by D-fructose 1,6‑biphosphate (FBP) and is inhibited by oxalate and 3,3',5-triiodo-L-thyronine (T3) (7, 8).

References

  1. Tani, K. et al. (1988) Gene 73:509.
  2. Noguchi, T. et al. (1986) J. Biol. Chem. 261:13807.
  3. Corcoran, E. et al. (1976). Biochim. Biophys. Acta 446:96.
  4. Brinck, U. et al. (1994). Virchows Arch. 424:177.
  5. Christofk, H.R. et al. (2008) Nature 452: 230.
  6. Dombrauckas, J.D. et al. (2005) Biochemistry 44:9417.
  7. Kato, H. et al. (1989) Proc. Natl. Acad. Sci. U.S.A. 86:7861.
  8. Ashizawa, K. et al. (1991) Biochemistry 30:7105.

Long Name

Pyruvate Kinase, Muscle

Alternate Names

CTHBP, OIP3, p58, PK2, PK3, TCB, THBP1, Tumor M2-PK

Entrez Gene IDs

5315 (Human); 18746 (Mouse); 25630 (Rat)

Gene Symbol

PKM

UniProt

P14618 (Human)

Additional PKM2 Products

Product Documents for Recombinant Human PKM2 Protein, CF

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Product Specific Notices for Recombinant Human PKM2 Protein, CF

For research use only

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