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Merck
모든 사진(4)

주요 문서

P6556

Sigma-Aldrich

Proteinase K from Tritirachium album

lyophilized powder, ≥30 units/mg protein

동의어(들):

Endopeptidase K

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
eCl@ss:
32160410
NACRES:
NA.54

양식

lyophilized powder

Quality Level

특이 활성도

≥30 units/mg protein

분자량

28.93 kDa

기술

DNA extraction: suitable

solubility

H2O: soluble 1 mg/mL, clear, colorless

외래 활성

Dnase ≤30 Kunitz units/mg solid
RNase ≤0.003 Kunitz units/mg solid

배송 상태

wet ice

저장 온도

−20°C

유사한 제품을 찾으십니까? 방문 제품 비교 안내

애플리케이션

Product P6556 is provided as a lyophilized powder. Product P6556 has been used to break down human lens protein. Protease footprinting by Proteinase K digestion can reveal protein-protein surface interactions. The enzyme from Sigma has been used in the pre-hybridization step of chicken embryos. It has also been used for the enrichment of PrPSc, a prion protein that is present in sheep, hamster and mouse scrapie samples.
Proteinase K is useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
It is used for the removal of endotoxins bound to cationic proteins such as lysozyme and ribonuclease A.
It is useful for the isolation of hepatic, yeast, and mung bean mitochondria
and is used to determine enzyme localization on membranes
It is used for the treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling and
for digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research. Product P6556 is provided as a lyophilized powder. Product P6556 has been used to break down human lens protein.
Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Useful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.
Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.
Reported useful for the isolation of hepatic, yeast, and mung bean mitochondria
Determination of enzyme localization on membranes
Treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.
Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research.

생화학적/생리학적 작용

Proteinase K has a broad specificity and degrades many proteins even in the native state. It mainly cleaves the peptide bond adjacent to the carboxyl group of aliphatic and aromatic amino acids with blocked α-amino groups. The optimum pH is between 7.5-9.0 and the isoelectric point is 8.9 Ca2+ (1-5 mM) is required for activation. Proteinase K is inhibited by diisopropyl fluorophosphate (DFIP), and phenylmethanesulfonyl fluoride (PMSF).
Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.

단위 정의

One unit will hydrolyze urea-denatured hemoglobin to produce color equivalent to 1.0 μmole of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent).

또한 이 제품과 함께 일반적으로 구입

제품 번호
설명
가격

픽토그램

Health hazardExclamation mark

신호어

Danger

유해 및 위험 성명서

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

표적 기관

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


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문서 라이브러리 방문

M M Kristjánsson et al.
European journal of biochemistry, 260(3), 752-760 (1999-04-02)
An extracellular serine proteinase purified from cultures of a psychrotrophic Vibrio species (strain PA-44) belongs to the proteinase K family of the superfamily of subtilisin-like proteinases. The enzyme is secreted as a 47-kDa protein, but under mild heat treatment (30
Rongzhu Cheng et al.
The Journal of biological chemistry, 279(44), 45441-45449 (2004-08-19)
We report here the isolation of a novel acid-labile yellow chromophore from the enzymatic digest of human lens proteins and the identification of its chemical structure by liquid chromatography-mass spectrometry, liquid chromatography-tandem mass spectrometry, and (1)H, (13)C, and two-dimensional NMR.
Nathaniel Denkers et al.
Developmental dynamics : an official publication of the American Association of Anatomists, 229(3), 651-657 (2004-03-03)
Multi-color whole-mount in situ hybridization is a powerful technique for comparing the spatial expression patterns of two or more genes in developing embryos. We have developed an amplified triple-label whole-mount fluorescence in situ hybridization (FISH) protocol that permits detection of
Michela Candelma et al.
Reproduction (Cambridge, England), 153(2), 123-132 (2016-11-03)
In vertebrates, the regulation of gametogenesis is under the control of gonadotropins (Gth), follicle-stimulating hormone (Fsh) and luteinizing hormone (Lh). In fish, the physiological role of Gths is not fully understood, especially in species with asynchronous ovarian development. To elucidate
Janus S Jakobsen et al.
Science advances, 5(7), eaaw4304-eaaw4304 (2019-07-17)
The key myeloid transcription factor (TF), CEBPA, is frequently mutated in acute myeloid leukemia (AML), but the direct molecular effects of this leukemic driver mutation remain elusive. To investigate CEBPA mutant AML, we performed microscale, in vivo chromatin immunoprecipitation sequencing

문서

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

프로토콜

Proteinase K (EC 3.4.21.64) activity can be measured spectrophotometrically using hemoglobin as the substrate. Proteinase K hydrolyzes hemoglobin denatured with urea, and liberates Folin-postive amino acids and peptides. One unit will hydrolyze hemoglobin to produce color equivalent to 1.0 μmol of tyrosine per minute at pH 7.5 at 37 °C (color by Folin & Ciocalteu's Phenol Reagent).

In Situ Hybridization of Whole-Mount Mouse Embryos with RNA Probes: Hybridization, Washes, and Histochemistry

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