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Merck

P5985

Protease from Bacillus sp.

liquid, ≥16 U/g

Synonim(y):

Everlase 16.0 L

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50 ML

569,00 zł

250 ML

1351,50 zł

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Informacje o tej pozycji

UNSPSC Code:
12352204
EC Number:
232-752-2
NACRES:
NA.54
MDL number:
Specific activity:
≥16 U/g
Biological source:
Bacillus sp.

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biological source

Bacillus sp.

form

liquid

specific activity

≥16 U/g

mol wt

20--30 kDa

storage temp.

2-8°C

Quality Level

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Ta pozycja
P3111P5860P0029
specific activity

≥16 U/g

specific activity

≥16 U/g

specific activity

≥8 U/g

specific activity

-

biological source

Bacillus sp.

biological source

Bacillus sp.

biological source

-

biological source

Bacillus sp.

form

liquid

form

liquid

form

liquid

form

granular

mol wt

20--30 kDa

mol wt

20-30 kDa

mol wt

20--30 kDa

mol wt

-

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

General description

Proteases are ubiquitously found in nature and microbes are the desired source for these enzymes.[1] They are classified into four classes namely aspartic, serine, cysteine and metalloproteases.[2]

Application

Protease from Bacillus sp. has been used to determine its proteolytic activity by spectrophotometric method.[3]

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.[2] 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.[1] 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.[2]

Legal Information

A product of Novozyme Corp.
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pictograms

Health hazardCorrosion

signalword

Danger

Hazard Classifications

Aquatic Chronic 3 - Eye Dam. 1 - Resp. Sens. 1

Klasa składowania

10 - Combustible liquids

wgk

WGK 2

ppe

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


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Isolation, production and characterization of protease from Bacillus sp. isolated from soil sample
Josephine FS, et al.
Journal of Microbiology, 2(1), 163-168 (2012)
Irreversible inhibitors of serine, cysteine, and threonine proteases
Powers JC, et al.
Chemical Reviews, 102(12), 4639-4750 (2002)
Effect of UV light on microbial proteases: From enzyme inactivation to antioxidant mitigation.
Lante A, et al.
Innovative Food Science & Emerging Technologies, 17, 130-134 (2013)
M Du et al.
Journal of animal science, 85(4), 919-927 (2006-12-21)
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
Laure El Chamy et al.
Nature immunology, 9(10), 1165-1170 (2008-08-30)
In drosophila, molecular determinants from fungi and Gram-positive bacteria are detected by circulating pattern-recognition receptors. Published findings suggest that such pattern-recognition receptors activate as-yet-unidentified serine-protease cascades that culminate in the cleavage of Spätzle, the endogenous Toll receptor ligand, and trigger

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