Proteinase from Aspergillus melleus

Type XXIII, ≥3 units/mg solid

CAS Number:
EC Number:
MDL number:

Quality Level





specific activity

≥3 units/mg solid

storage temp.


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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.


5, 25 g in glass bottle

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.


Exclamation markHealth hazard

Signal Word


Hazard Statements

Precautionary Statements

Target Organs

Respiratory system

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
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...
Ravindra S Prajapati et al.
Development (Cambridge, England), 146(24) (2019-12-07)
During early embryogenesis, the ectoderm is rapidly subdivided into neural, neural crest and sensory progenitors. How the onset of lineage determinants and the loss of pluripotency markers are temporally and spatially coordinated in vivo is still debated. Here, we identify...
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...
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...
To standardize a procedure for the enzymatic assay of Protease using Casein as a substrate.
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