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High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong


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High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong Detail:

No.1 liquid

Protein specific activity>800U/mL, the concentration is 20mg/mL, no Nickase residue

No.2 powder

Appearance White lyophilized powder
Electrophoretic purity ≥95%
Enzyme activity ≥30U/mg
Nucleic acid residue Invisible
Deoxyribonuclease residue Invisible
Ribonuclease residue Invisible
Cart No. G1205-10ML
Storage When stored at –20 °C, the product retains activity for at least 1 years, ice bag transportation.

Proteinase K is a serine protease belonging to the subtilisin family with efficient enzymatic activity and broad substrate specificity, which preferentially decomposes ester bonds and peptides adjacent to the C-terminus of hydrophobic amino acids, sulfur-containing amino acids, and aromatic amino acids bonds, which are often used to degrade proteins to produce short peptides. Proteinase K has the characteristic of the typical catalytic triad Asp39-His69-Ser224 unique to serine proteases and has two Ca2+ binding sites around the active center to increase its stability and maintain high enzymatic activity under a wider range of conditions.

1. Genetic diagnosis kit.
2. RNA and DNA extraction kits.
3. Extract non-protein components in tissues and degrade protein impurities (such as preparation of DNA vaccines and heparin).
4. Preparation of Chromosomal DNA for Pulse Electrophoresis.
5. Western blotting.
6. Development and production of enzymatic glycated albumin reagents in the field of in vitro diagnostics.

1. 30mg/bottle 1g/bottle or 100g/bottle
2. 1kgs/foil bag

Proteinase K is a stable serine protease with broad substrate specificity. It degrades many proteins in the native state even in the presence of detergents. It is not activated by metal ions, chelating agents (for example, EDTA), sulfhydryl reagents, or by tripsin or chymotrypsin inhibitors. It is stable over a wide pH range (4–12.5), with optimal activity at pH 6.5–9.5. Activity can be stimulated by addition of denaturing agents (SDS and Urea). Rapid denaturation of the enzyme occurs at temperature above 70°C. Autolysis of the enzyme occurs increasingly at alkaline pH. However, Proteinase K is not completely inactivated by autolysis. Some enzyme fragments continue to maintain their complete proteolytic activity, even after extensive autolysis. Proteinase K is frequently used in molecular biology applications to digest unwanted proteins, such as nucleases in DNA or RNA preparations from microorganisms, cultured cells, and plants. The enzyme is typically used at 50–200 ug/ml in nucleic acid preparations at pH 7.5–8.0 and 37~55oC. Incubation times vary from 30 minutes to 18 hours.

A stable and highly reactive serine protease; used for protein and nucleic acid isolation.Proteinase K is used in the purification of RNA and DNA from tissues or cell lines.


Product detail pictures:

High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong detail pictures

High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong detail pictures

High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong detail pictures

High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong detail pictures


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We normally follow the basic principle "Quality Initial, Prestige Supreme". We've been fully committed to offering our consumers with competitively priced good quality merchandise, prompt delivery and professional support for High Quality 107-36-8 - Proteinase K with cas 39450-01-6 – Unilong , The product will supply to all over the world, such as: Qatar, Hanover, Madrid, Our products are widely recognized and trusted by users and can meet continuously changing of economic and social needs. We welcome new and old customers from all walks of life to contact us for future business relationships and mutual success!
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    5 Stars By Matthew Tobias from Puerto Rico - 2018.11.28 16:25
    Good quality, reasonable prices, rich variety and perfect after-sales service, it's nice!
    5 Stars By Joa from UK - 2018.07.27 12:26
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