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Merck

A6362

Sigma-Aldrich

Alpha-lytic protease

Szinonimák:

Alpha-lytic endopeptidase, alphaLP

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Enzyme Commission szám:
UNSPSC kód:
12352204
NACRES:
NA.54

biológiai forrás

bacterial

Minőségi szint

form

liquid

specifikus aktivitás

≥0.0005 U/mg

molekulatömeg

19,860 Da

optimális pH

5.0(storage)
7.5(activity)

pI 

9.69

kiszállítva

dry ice

tárolási hőmérséklet

−70°C

Általános leírás

Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It generates peptides of similar average length as trypsin.

aLP was first isolated from the myxobacterium Lysobacter enzymogenes. The pro-form of aLP is 397 amino acids long. In its mature form, aLP is 198 amino acids long. Its tertiary structural core resembles those of pancreatic serine proteases.

Crystal structure studies of aLP have been reported. Several studies are available on the active site and catalytic mechanism of aLP. The role of the pro-region in the activation, secretion and folding of aLP has been studied.

The activity of aLP in the presence of various solution components is as follows:
  • 0.1% sodium deoxycholate: ~1.75-fold enhanced activity
  • 1.0% sodium deoxycholate: ~60% activity
  • 0.1% SDS: ~50% activity
  • 1.0% SDS: ~40% activity
  • 1 M guanidine HCl: ~20% activity
  • 4 M guanidine HCl: ~1% activity (essentially inactivated)

Egység definíció

One unit will produce one mmole of p-nitroaniline per minute from N-succinyl-Ala-Ala-Ala-PNA at 25 °C at pH 7.5

Fizikai forma

Supplied as a solution in 10 mM sodium acetate buffer, pH 5.0.

Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

Molecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8 Angstroms resolution.
G D Brayer et al.
Journal of molecular biology, 131(4), 743-775 (1979-07-15)
Hangping Yao et al.
Cell, 183(3), 730-738 (2020-09-28)
SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, the detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic
C A Bauer et al.
European journal of biochemistry, 120(2), 289-294 (1981-11-01)
The active site of alpha-lytic protease has been studied with a number of synthetic peptides and compared with similar data published for elastase. The kinetic data indicate that the active site of alpha-lytic protease extends over at least six subsites
M Fujinaga et al.
Journal of molecular biology, 184(3), 479-502 (1985-08-05)
The structure of alpha-lytic protease, a serine protease produced by the bacterium Lysobacter enzymogenes, has been refined at 1.7 A resolution. The conventional R-factor is 0.131 for the 14,996 reflections between 8 and 1.7 A resolution with I greater than
Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern.
Shajahan, et al.
Scientific Reports, 13, 10053-10053 (2023)

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