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Merck

CK-RO

Roche

Creatine Kinase (CK)

from rabbit muscle

Sinonimo/i:

creatine phosphokinase

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Informazioni su questo articolo

UNSPSC Code:
12352204
Numero CE:
NACRES:
NA.54
Biological source:
rabbit muscle

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biological source

rabbit muscle

form

lyophilized

packaging

pkg of 100 mg (10127566001), pkg of 500 mg (10736988001)

manufacturer/tradename

Roche

color

white to light yellow

optimum pH

6.0-7.0(reverse reaction), 9.0(forward reaction)

solubility

water: soluble

suitability

suitable for immunoprecipitation

NCBI accession no.

UniProt accession no.

application(s)

life science and biopharma
sample preparation

foreign activity

ATPase <0.001%, HK <0.001%, myokinase <0.001%

storage temp.

2-8°C

Gene Information

rabbit ... CKM(100009056)

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Questo articolo
MAK116CRPHO-ROC0984
Creatine Kinase (CK) from rabbit muscle

Roche

CK-RO

Creatine Kinase (CK)

Creatine phosphate crystalline, &gt;97%

Roche

CRPHO-RO

Creatine phosphate

Gene Information

rabbit ... CKM(100009056)

Gene Information

human ... CKB(1152), CKM(1158)
mouse ... CKB(12709), CKM(12715)
rat ... CKB(24264), CKM(24265)

Gene Information

-

Gene Information

human ... CKB(1152), CKM(1158)

biological source

rabbit muscle

biological source

-

biological source

-

biological source

human heart

form

lyophilized

form

-

form

crystalline

form

liquid

suitability

suitable for immunoprecipitation

suitability

-

suitability

-

suitability

suitable for tissue

application(s)

life science and biopharma
sample preparation

application(s)

-

application(s)

-

application(s)

pharmaceutical

solubility

water: soluble

solubility

-

solubility

-

solubility

-

General description

at 25 °C (800 U/mg lyophilizate at 37 °C) with creatine phosphate and ADP as the substrates, and N-acetyl-L-cysteine as the activator.

Application

Creatine kinase has been used as a component of translation buffer used in in vitro translation assay[1] and as a component of energy regeneration mix.[2]

Biochem/physiol Actions

Creatine kinase (CK) is a guanidino-kinase that catalyzes the reversible phosphorylation of creatine to phosphocreatine at the expense of ATP. It plays crucial roles in rapid regeneration of ATP in cells with high demand for energy. Increased level of CK in human blood indicates diseases of the nervous system and the heart muscle, malignant hypothermia, and certain tumors. Metals such as Mg, Mn and Ca act as cofactors for CK. It also forms a substrate for protein kinase C, an important signaling molecule involved in cell growth. A product of enzymatic reaction of CK, phosphocreatine, is found to prevent HIV (human immunodeficiency virus) replication in macrophages.[3]

Features and Benefits

Specific activity: Approximately 350U/mg lyophilizate at +25°C (800U/mg lyophilizate at +37°C) with creatine phosphate and ADP as the substrates, and N-acetyl-L-cysteine as activator.

Physical form

Lyophilizate, stabilized

Preparation Note

Storage conditions (working solution): Working solutions and storage conditions in routine applications:
Dissolve in 0.1 M imidazole buffer; aliquot and store at -15 to -25 °C.
Stable for approximately four weeks at -15 to -25 °C.
Avoid repeated freezing and thawing.

Dissolve in 0.5% NaHCO3 solution.
Do not freeze. Store protected from light.
Stable for 2 - 3 days, when stored at 2 to 8 °C.
Or
Dissolve in 30 mM glycine buffer, pH 9.0, with 0.2 mM DTT.
Stable for 2 - 3 days, when stored at 2 to 8 °C.

Analysis Note

Contaminants: <0.001% ATPase, HK, and myokinase, each

Other Notes

For life science research only. Not for use in diagnostic procedures.
One unit CK activity (+25 °C) = 2.3 U (+37 °C), creatin-P and ADP as substrates, NAcCys as reactivator.

Classe di stoccaggio

11 - Combustible Solids

wgk

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash


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Irina M Kuznetsova et al.
Biochimica et biophysica acta, 1596(1), 138-155 (2002-05-02)
GdmCl-induced unfolding of rabbit muscle creatine kinase, CK, has been studied by a variety of physico-chemical methods including near and far UV CD, SEC, intrinsic fluorescence (intensity, anisotropy and lifetime) as well as intensity and lifetime of bound ANS fluorescence.
Aurélie M Rakotondrafara et al.
Nature protocols, 6(5), 563-571 (2011-04-30)
Much of the regulation of gene expression occurs at the level of protein synthesis. In addition to the canonical translation factors, a multitude of proteins and microRNAs (miRNAs) act as regulatory trans-acting factors. Mechanistic analysis of translational control benefits from
J K Rao et al.
FEBS letters, 439(1-2), 133-137 (1998-12-16)
The crystal structure of rabbit muscle creatine kinase, solved at 2.35 A resolution by X-ray diffraction methods, clearly identified the active site with bound sulfates surrounded by a constellation of arginine residues. The putative binding site of creatine, which is
Marta Teperek et al.
International journal of molecular sciences, 15(9), 16719-16740 (2014-09-23)
Spermatozoa are more efficient at supporting normal embryonic development than spermatids, their immature, immediate precursors. This suggests that the sperm acquires the ability to support embryonic development during spermiogenesis (spermatid to sperm maturation). Here, using Xenopus laevis as a model
Marta Teperek et al.
Genome research, 26(8), 1034-1046 (2016-04-02)
For a long time, it has been assumed that the only role of sperm at fertilization is to introduce the male genome into the egg. Recently, ideas have emerged that the epigenetic state of the sperm nucleus could influence transcription

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