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Safety Information

P9208

Sigma-Aldrich

Polymyxin Acylase from Pseudomonas sp.

≥0.1 units/mg solid

Synonym(s):

Peptide N-fatty acylase

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200 MG
¥193,000

¥193,000

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200 MG
¥193,000

About This Item

CAS Number:
111174-43-7
MDL number:
MFCD00286307
UNSPSC Code:
12352204
NACRES:
NA.54

¥193,000

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biological source

bacterial (Pseudomonas spp.)

Quality Level

200

form

solid

specific activity

≥0.1 units/mg solid

relevant disease(s)

cancer

storage temp.

−20°C

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Application

Polymyxin acylase, from Pseudomonas sp., is a N-myristoyl cleaving enzyme that has been used to determine the N-myristoyl peptide sequence [1] and may be useful in cancer research since it has antitumor activity against murine and human tumor cells [2].

Biochem/physiol Actions

Polymyxin acylase, from Pseudomonas sp. deacylates polymyxin group antibiotics and long-chain fatty acyl groups of proteins. Polymyxin acylase has an affinity for long-chain fatty acyl proteins in human carcinoma cells [2].

Quality

Crude actone powder;

Unit Definition

One unit will hydrolyze 1 μmole of N-octanoyl-5-aminovaleric acid per min at pH 8.0 at 37°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

P9208-200MG-PW:
P9208-VAR:
P9208-BULK:
P9208-200MG:

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Certificates of Analysis (COA)

Lot/Batch Number
SLCF4395
SLCD7626
SLBZ8605
SLBT7841
SLBJ4412V

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N Yasuda et al.
Biological & pharmaceutical bulletin, 18(4), 615-617 (1995-04-01)
Polymyxin acylase from Pseudomonas sp. M-6-3 can deacylate not only polymyxin group antibiotics, but also the long-chain fatty acyl group of proteins and peptides. We found the in vitro antitumor activity of polymyxin acylase against murine and human tumor cells
S Misumi et al.
Biochemical and biophysical research communications, 217(2), 632-639 (1995-12-14)
Polymyxin acylase isolated from Pseudomonas sp. M-6-3 was used as an N-myristoyl cleaving enzyme in order to determine a part of the N-terminal amino acid sequence of N-myristoyl proteins. The enzyme hydrolyzed a number of N-myristoyl oligopeptides at various hydrolysis

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