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Merck

1.07393

Proteinase K

(from Tritirachium album) solution in Tris/HCl pH 7.5; 0.01 mol/l; 600 mAnson-U/ml; for molecular biology EC 3.4.21.14

別名:

ProK, native proteinase K solution, non-specific protease

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この商品について

NACRES:
NA.51
UNSPSC Code:
12352204

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製品名

Proteinase K, (from Tritirachium album) solution in Tris/HCl pH 7.5; 0.01 mol/l; 600 mAnson-U/ml; for molecular biology EC 3.4.21.14

form

liquid

pH

7.5 (25 °C in H2O, undiluted)

density

1.10 g/cm3 at 20 °C

storage temp.

2-8°C

Quality Level

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当該品目
1.24568RPROTKSOL-RORPROTK-RO
form

liquid

form

solid

form

buffered aqueous solution (18 ± mg/mL; pH 7.5)

form

lyophilized

pH

7.5 (25 °C in H2O, undiluted)

pH

6.2-6.8 (20 °C, 10 g/L in H2O)

pH

-

pH

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

400

Quality Level

400

Quality Level

100

Quality Level

100

density

1.10 g/cm3 at 20 °C

density

1.1 g/cm3

density

-

density

-

Analysis Note

Appearance (colour): colourless
Appearance (clearness): clear
Activity (hemoglobin; pH 7.5; 37 °C): ≥ 600 mAnsonU/ml
Spec. activity (calc. on protein): ≥ 40.0 mAnsonU/mg
DNases (Nicking activity; pBR 322; 6 h; 37 °C): not detectable
RNases (RNA; 2 h; 37°C): not detectable
Colony count (aerobic bacteria): ≤ 10 CFU/ml

Application

Proteinase K has been used:
  • to de-crosslink immunoprecipitated samples
  • to treat the poly-L-lysine coated slides of colon tissues for terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) assay
  • in in situ hybridization

Biochem/physiol Actions

Proteinase K catalyzes the hydrolysis of esters and peptide bonds. It is used with non-aqueous hydrated solvents for synthesizing peptides. Proteinase K is used to break the cross-linking that develops secondary to formalin fixation and expose the target sequence for primers and polymerase.

General description

Proteinase K is an endopeptidase that belongs to the subtilisin family of proteinases. The polypeptide chain contains 278 amino acids with the catalytic triad Asp39, His69, Ser224.

Hazard Classifications

Resp. Sens. 1

pictograms

Health hazard

signalword

Danger

hcodes

保管分類

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


試験成績書(COA)

製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。

以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

F Chavagnat et al.
Applied and environmental microbiology, 65(7), 3001-3007 (1999-07-02)
The general aminopeptidase PepN from Streptococcus thermophilus A was purified to protein homogeneity by hydroxyapatite, anion-exchange, and gel filtration chromatographies. The PepN enzyme was estimated to be a monomer of 95 kDa, with maximal activity on N-Lys-7-amino-4-methylcoumarin at pH 7
María Isabel Navarro-Mendoza et al.
Current biology : CB, 29(22), 3791-3802 (2019-11-05)
Centromeres are rapidly evolving across eukaryotes, despite performing a conserved function to ensure high-fidelity chromosome segregation. CENP-A chromatin is a hallmark of a functional centromere in most organisms. Due to its critical role in kinetochore architecture, the loss of CENP-A

資料

Balancing Proteinase K cost with quality and technical support ensures optimal enzyme selection for diverse applications.

Guidelines on use of proteinase K, an enzyme commonly used to degrade proteins, and protect DNA and RNA from degradation in samples.

In blood DNA extraction, Proteinase K, an enzyme commonly used to degrade proteins, can help break down the cellular and nuclear membranes, releasing DNA from the cells that protect it from degradation and increase purity/yield making it more suitable for various molecular biology techniques.

Proteinase K aids in molecular biology applications by digesting structural proteins, removing nucleases, and isolating intact genomic DNA.

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