P5985
Protease from Bacillus sp.
liquid, ≥16 U/g
Sinónimos:
Everlase 16.0 L
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About This Item
Productos recomendados
biological source
Bacillus sp.
form
liquid
specific activity
≥16 U/g
mol wt
20--30 kDa
storage temp.
2-8°C
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General description
Proteases are ubiquitously found in nature and microbes are the desired source for these enzymes. They are classified into four classes namely aspartic, serine, cysteine and metalloproteases.
Application
Protease from Bacillus sp. has been used to determine its proteolytic activity by spectrophotometric method.
Biochem/physiol Actions
Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Proteases, secreted from Bacillus sp., typically have molecular weights ranging from 20,000 to 30,000. They are typically stabilized by Ca2+ and have high isoelectric points. It is highly soluble in detergents at a wide range of pH and temperatures. Protease improves healing process by efficiently removing necrotic materials from wounds. It is extensively used in laundry detergents to remove protein based stains from clothing. In addition, protease is also used in food, pharmaceutical, leather and silk industries. It is a key constituent in biopharmaceutical products including contact-lens enzyme cleaners and enzymatic deriders. Proteases also aid in various physiological processes such as protein turnover, digestion, blood coagulation, fertilization and cell differentiation. It also facilitates growth, cell signaling, the immune response, and apoptosis.
Legal Information
A product of Novozyme Corp.
signalword
Danger
hcodes
Hazard Classifications
Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificados de análisis (COA)
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Journal of Microbiology, 2(1), 163-168 (2012)
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Proceedings of the National Academy of Sciences of the United States of America, 106(30), 12442-12447 (2009-07-11)
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Mammalian target of rapamycin (mTOR) signaling is one of the main signaling pathways controlling protein synthesis. Leucine treatment upregulates mTOR signaling, which enhances protein synthesis; however, the mechanisms are not well understood. Herein, treatment of C2C12 myoblast cells with leucine
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