P4032
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:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-642-4
NACRES:
NA.54
MDL number:
Product Name
Proteinase from Aspergillus melleus, Type XXIII, ≥3 units/mg solid
biological source
Aspergillus sp. (A. melleus)
type
Type XXIII
form
solid
specific activity
≥3 units/mg solid
storage temp.
2-8°C
Quality Level
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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 .
Other Notes
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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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
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
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
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