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P4032

Sigma-Aldrich

Proteinase from Aspergillus melleus

Type XXIII, ≥3 units/mg solid

Synonym(s):

Protease from Aspergillus melleus, Proteinase from Aspergillus sp.

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About This Item

CAS Number:
9001-92-7
EC Number:
232-642-4
MDL number:
MFCD00132092
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Aspergillus sp. (A. melleus)

Quality Level

200

type

Type XXIII

form

solid

specific activity

≥3 units/mg solid

storage temp.

2-8°C

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Application

Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. Proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. Proteinase is used in nucleic acid isolation procedures in incubations. It is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. Product P4032 is from Aspergillus melleus and has been used to non-specifically degraded xylanase from Streptomyces halstedii.

Biochem/physiol Actions

Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate .

Unit Definition

One unit will hydrolyze casein to produce color equivalent to 1.0 μmole (181 μg) of tyrosine per min at pH 7.5 at 37 °C (color by Folin-Ciocalteu reagent), unless otherwise indicated.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Chenzhong Yin et al.
Scientific reports, 10(1), 15078-15078 (2020-09-17)
Understanding the mechanisms by which neurons create or suppress connections to enable communication in brain-derived neuronal cultures can inform how learning, cognition and creative behavior emerge. While prior studies have shown that neuronal cultures possess self-organizing criticality properties, we further
Martin Steinhoff et al.
Endocrine reviews, 26(1), 1-43 (2005-02-04)
Serine proteinases such as thrombin, mast cell tryptase, trypsin, or cathepsin G, for example, are highly active mediators with diverse biological activities. So far, proteinases have been considered to act primarily as degradative enzymes in the extracellular space. However, their
J C Groot et al.
The British journal of nutrition, 79(6), 519-525 (1998-10-15)
Differences between the fermentation characteristics of cell contents (CC) and protease-treated cell walls (CW) of young leaves of Italian ryegrass (Lolium multiflorum Lam.) cultivar Multimo (tetraploid), were studied in vitro. Gas and volatile fatty acid (VFA) production rates were measured
José M Fernández-Abalos et al.
Microbiology (Reading, England), 149(Pt 7), 1623-1632 (2003-07-12)
The xylanase Xys1L from Streptomyces halstedii JM8 is known to be processed extracellularly, to produce a protein of 33.7 kDa, Xys1S, that retains catalytic activity but not its cellulose-binding capacity. This paper demonstrates that at least five serine proteases isolated
Mikhail E Kandel et al.
Nature communications, 10(1), 4691-4691 (2019-10-18)
Multiple scattering and absorption limit the depth at which biological tissues can be imaged with light. In thick unlabeled specimens, multiple scattering randomizes the phase of the field and absorption attenuates light that travels long optical paths. These obstacles limit
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Protocols

Enzymatic Assay of Protease Using Casein As a Substrate

To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate.

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