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P9136

Sigma-Aldrich

Pyruvate Kinase from rabbit muscle

Type III, lyophilized powder, 350-600 units/mg protein

Synonym(s):

ATP:pyruvate 2-O-phosphotransferase, PK

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CN¥752.91
5000 UNITS
CN¥1,858.10
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CN¥7,039.08
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CN¥10,334.67

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Estimated to ship onOctober 16, 2025Details

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1000 UNITS
CN¥752.91
5000 UNITS
CN¥1,858.10
25000 UNITS
CN¥7,039.08
50000 UNITS
CN¥10,334.67

About This Item

CAS Number:
9001-59-6
Enzyme Commission number:
2.7.1.40 (BRENDA, IUBMB)
EC Number:
232-616-2
MDL number:
MFCD00081946
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

CN¥752.91

List PriceCN¥941.13Save 20%

Estimated to ship onOctober 16, 2025Details

Request a Bulk Order

biological source

rabbit muscle

Quality Level

200

type

Type III

form

lyophilized powder

specific activity

350-600 units/mg protein

mol wt

237 kDa

foreign activity

lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%

storage temp.

−20°C

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Pyruvate Kinase from rabbit muscle Type III, lyophilized powder, 350-600 units/mg protein

P9136

Pyruvate Kinase from rabbit muscle

Pyruvate Kinase from rabbit muscle Type VII, buffered aqueous glycerol solution, 350-600 units/mg protein

P7768

Pyruvate Kinase from rabbit muscle

Pyruvate Kinase from Bacillus stearothermophilus Type VIII, lyophilized powder, 100-300 units/mg protein

P1903

Pyruvate Kinase from Bacillus stearothermophilus

Pyruvate Kinase from rabbit muscle Type II, ammonium sulfate suspension, 350-600 units/mg protein

P1506

Pyruvate Kinase from rabbit muscle

specific activity

350-600 units/mg protein

specific activity

350-600 units/mg protein

specific activity

100-300 units/mg protein

specific activity

350-600 units/mg protein

biological source

rabbit muscle

biological source

-

biological source

Bacillus sp. (B. stearothermophilus)

biological source

rabbit muscle

form

lyophilized powder

form

buffered aqueous glycerol solution

form

lyophilized powder

form

ammonium sulfate suspension

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

mol wt

237 kDa

mol wt

237 kDa

mol wt

-

mol wt

237 kDa

foreign activity

lactic dehydrogenase, creatine phosphokinase, phosphoglucomutase, and myokinase ≤0.01%

foreign activity

lactic dehydrogenase and creatine phosphokinase ≤0.01%, phosphoglucomutase and myokinase ≤0.05%

foreign activity

-

foreign activity

lactic dehydrogenase, creatine phosphokinase, and myokinase ≤0.01%, phosphoglucomutase ≤0.05%

General description

Pyruvate Kinase (PK) is a glycolysis enzyme[1] and has four isozymes L, R, M1, and M2. The L isozyme is localized in gluconeogenic tissues, particularly in the liver. Whereas the R and M1 are localized in the adult skeletal muscles, heart, brain and erythrocytes, respectively.[2] M2 is localized in the nucleus of the cells.[1]

Application

Pyruvate Kinase from rabbit muscle has been used to convert adenosine diphosphate (ADP) to adenosine triphosphate (ATP) in Pseudomonas putida cells.[3]
Pyruvate kinase has been used in plant spectrophotometric assays to measure ATP hydrolysis [4]. Pyruvate kinase is also used to study pyruvate kinase (PK) deficiency [5].

Biochem/physiol Actions

Molecular Weight: 237 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa.
Isoelectric Point: 7.6
Optimal pH: ∼7.5
Optimal Temperature: 25°C
ΕA280 = 0.54 for 1 mg(p)/ml, 1 cm path
Reported KM values are ATP (0.86 mM), pyruvate (10 mM), ADP (0.3 mM), and PEP (0.07 mM) in Tris buffer at pH 7.4 and 30 °C. Pyruvate kinase is highly specific for phosphoenolpyruvate, but can utilize other dinucleotide triphosphates as substrates in place of ATP including GTP, ITP, dATP, UTP, and CTP.
Pyruvate kinase (PK) catalyzes an important process of transferring phosphate group from phosphoenolpyruvate (PEP) to adenosine diphosphate (ADP). This reaction results in the conversion of PEP to pyruvate and adenosine triphosphate (ATP).[1][6] Pyruvate kinase plays a major role in glycolysis and gluconeogenesis.[1][7] High levels of pyruvate kinase M2 (PKM2) inhibits cell proliferation and tumor growth.[8] Deficiency of PK in red blood cells (RBC) leads to non-spherocytic hemolytic anaemia.[9] In human erythrocytes, deficiency of PK induces a protective effect against Plasmodium falciparum.[6]

Unit Definition

One unit will convert 1.0 μmole of phospho(enol)pyruvate to pyruvate per min at pH 7.6 at 37 °C.

Analysis Note

Protein determined by biuret.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品
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    SLCD4181
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    Anoxic metabolism and biochemical production in Pseudomonas putida F1 driven by a bioelectrochemical system
    Lai B, et al.
    Biotechnology for Biofuels, 9(1), 39-39 (2016)
    Pyruvate kinase deficiency and malaria
    Ayi K, et al.
    The New England Journal of Medicine, 358(17), 1805-1810 (2008)
    S P Robinson et al.
    Plant physiology, 88(4), 1008-1014 (1988-12-01)
    Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco) activase protein was purified from spinach leaves by ammonium sulfate precipitation and ion exchange fast protein liquid chromatography. This resulted in 48-fold purification with 70% recovery of activity and yielded up to 18 milligrams of rubisco
    Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis
    Anastasiou D, et al.
    Nature Chemical Biology, 8(10), 839-839 (2012)
    Pyruvate kinase M2 regulates gene transcription by acting as a protein kinase
    Gao X, et al.
    Molecular Cell, 45(5), 598-609 (2012)
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