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P1506

Pyruvat-Kinase aus Kaninchenmuskel

Type II, ammonium sulfate suspension, 350-600 units/mg protein

Synonym(e):

ATP:pyruvate 2-O-phosphotransferase, PK, Phospho-enolpyruvat-Kinase

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1000 UNITS

€ 44,60

5000 UNITS

€ 137,00

25000 UNITS

€ 528,00

50000 UNITS

€ 787,00

€ 44,60


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Über diesen Artikel

CAS-Nummer:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
EG-Nummer:
MDL number:
Specific activity:
350-600 units/mg protein
Biological source:
rabbit muscle

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biological source

rabbit muscle

type

Type II

form

ammonium sulfate suspension

specific activity

350-600 units/mg protein

mol wt

237 kDa

storage condition

(Tightly closed)

technique(s)

ligand binding assay: suitable

color

white

foreign activity

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

storage temp.

2-8°C

Quality Level

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Dieser Artikel
SRP0414SRP0413P9136
biological source

rabbit muscle

biological source

human

biological source

human

biological source

rabbit muscle

technique(s)

ligand binding assay: suitable

technique(s)

-

technique(s)

-

technique(s)

-

specific activity

350-600 units/mg protein

specific activity

-

specific activity

-

specific activity

350-600 units/mg protein

form

ammonium sulfate suspension

form

aqueous solution

form

aqueous solution

form

lyophilized powder

mol wt

237 kDa

mol wt

59 kDa

mol wt

63 kDa

mol wt

237 kDa

storage temp.

2-8°C

storage temp.

−70°C

storage temp.

−70°C

storage temp.

−20°C

General description

Research Area: Cell Signaling

Pyruvate kinase from rabbit muscle catalyzes ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate.[1]Pyruvate kinase, an enzyme,[2] is found in a tetrameric or a dimeric form.[3] PKM1, PKM2, PKR, and PKL are the four mammalian pyruvate kinase isoforms.[2]

Application

Pyruvate kinase from rabbit muscle has been used in:

  • a structural study to understand the reaction mechanism of the final step in glycolysis. [4]
  • a study to investigate ATP-dependent phosphorylation of α-substituted carboxylic acids. [1]
  • enzyme assays.[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 from rabbit muscle can be activated by histidine and inhibited by low levels of zinc (Zn2+). [6] In the glycolytic pathway, pyruvate kinase (PK) functions as a terminal enzyme, catalyzing the conversion of phosphoenolpyruvate to pyruvate and the synthesis of ATP through substrate-level phosphorylation. Tetrameric structures of PK are more active and have a high affinity for phosphoenolpyruvate (PEP), whereas dimeric structures are less active and have a low affinity for PEP.[3] PK from rabbit muscle possesses positive kinetic cooperativity (Hill coefficient> 1.35) of the phosphoenol pyruvate and adenosine diphosphate(ADP) binding sites.[7]

Physical form

Suspension in 3.2 M (NH4)2SO4 solution, pH 6

Analysis Note

Protein determined by biuret.

Other Notes

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

Lagerklasse

12 - Non Combustible Liquids

wgk

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Zulassungslistungen

Zulassungslistungen werden hauptsächlich für chemische Produkte erstellt. Für nicht-chemische Produkte können hier nur begrenzte Angaben gemacht werden. Kein Eintrag bedeutet, dass keine der Komponenten gelistet ist. Es liegt in der Verantwortung des Benutzers, die sichere und legale Verwendung des Produkts zu gewährleisten.

7783-20-2

CAS No.

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Analysenzertifikate (COA)

Lot/Batch Number

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Die Dokumentenbibliothek aufrufen

Xun Chen et al.
Cancer cell international, 20(1), 523-523 (2020-12-10)
Pyruvate kinase is a terminal enzyme in the glycolytic pathway, where it catalyzes the conversion of phosphoenolpyruvate to pyruvate and production of ATP via substrate level phosphorylation. PKM2 is one of four isoforms of pyruvate kinase and is widely expressed
D E Ash et al.
Archives of biochemistry and biophysics, 228(1), 31-40 (1984-01-01)
Pyruvate kinase from rabbit muscle catalyzes an ATP-dependent phosphorylation of glycolate to yield 2-phosphoglycolate (F. J. Kayne (1974) Biochem. Biophys. Res. Commun. 59, 8-13). An investigation of anologous reactions with other alpha-substituted carboxylic acids reveals several new substrates for such
Glucokinase in Atlantic Halibut (Hippoglossus hippoglossus) Brockmann Bodies
Tranulis MA, et al.
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 116, 367-370 (1997)
Inhibitory effect of Zn2+ on rabbit muscle pyruvate kinase and reactivation by histidine.
Tamaki N.
J. Nutr. Sci. Vitaminol., 27, 107-116 (1981)
S Strumilo et al.
Zhurnal evoliutsionnoi biokhimii i fiziologii, 51(2), 103-107 (2015-06-02)
Some catalytic and kinetic properties of pyruvate kinase (PK, EC 2.7.1.40) isolated from the heart and skeletal muscles of rabbits and hares with a 9-16-fold purification were studied. The initial specific activity of the enzyme in hare heart homogenates was

Artikel

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Verwandter Inhalt

Questions

1–2 of 2 Questions  
  1. この製品(P1506, ピルビン酸キナーゼ)についてご質問があります。 この製品の比活性は350-600 units/mg proteinと記載ありますが、濃度としてU/mLはお分かりになるのでしょうか。 Lot毎に異なることかもしれませんので、試薬の瓶そのものに記載があったりするのでしょうか(データシートには記載が見当たらない)。 ご確認のほど、よろしくお願いいたします。

    1 answer
    1. The concentration in U/mL can be determined using the Enzymatic Activity and the mg protein/mL value reported on the lot specific Certificate of Analysis. For example, a lot has a reported Enzymatic Activity of 359 units/ mg protein and 13.7 mg protein/ mL will have a concentration 4918.3 units/ml. Please see the link below to review a sample or lot specific Certificate:
      https://www.sigmaaldrich.com/US/en/product/sigma/p1506#product-documentation

      Helpful?

  2. Hi, How long can this be stored in the fridge?

    1 answer
    1. This product is not assigned an expiration date or retest date. Products that are robust in nature and extremely stable, in the original unopened container, are not assigned an expiration date or retest schedule. These products will have no dating reported on either the label or the Certificate of Analysis. Products that are not assigned an expiration or retest date are covered by a warranty period of 1 year from the date of product shipment.

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