A3010
Acylase I from porcine kidney
Grade I, lyophilized powder, ≥1500 units/mg protein
Synonym(s):
Aminoacylase, N-Acylamino acid amidohydrolase
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-732-3
MDL number:
Specific activity:
≥1500 units/mg protein
type
Grade I
Quality Level
form
lyophilized powder
specific activity
≥1500 units/mg protein
composition
Protein, ≥60%
UniProt accession no.
storage temp.
−20°C
Gene Information
pig ... ACY1(396930)
Looking for similar products? Visit Product Comparison Guide
Application
Acylase I from porcine kidney has been used to study the acylase I-catalyzed deacetylation of various S-alkyl-N-acetyl-L-cysteines and their carbon and oxygen analogues . Acylase I may be useful to catalyze N-acetyl amino acids to enantiomerically pure L-amino acids .
Biochem/physiol Actions
Acylase I catalyzes the deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. n-Butylmalonic acid is an inhibitor of acylase I. S-alkyl-N-acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents have been found to be good acylase I substrates .
Analysis Note
Protein determined by biuret.
Other Notes
One unit will hydrolyze 1.0 μmole of N-acetyl-L-methionine per hr at pH 7.0 at 25 °C.
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
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
动植物源性产品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Jinit Masania et al.
Oxidative medicine and cellular longevity, 2019, 4851323-4851323 (2019-12-13)
Glycation, oxidation, nitration, and crosslinking of proteins are implicated in the pathogenic mechanisms of type 2 diabetes, cardiovascular disease, and chronic kidney disease. Related modified amino acids formed by proteolysis are excreted in urine. We quantified urinary levels of these
Y Fukagawa et al.
The Journal of antibiotics, 33(6), 543-549 (1980-06-01)
PS-5 was deacetylated to NS-5 (deacetylated PS-5) by l-amino acid acylase from porcine kidney and D-amino acid acylase from Streptomyces olivaceus but not by l-amino acid acylase from Aspergillus sp. Using PS-5, N-chloroacetyl-l-phenylalanine and N-chloroacetyl-D-valine as substrates, acylase producers were
V Uttamsingh et al.
Chemical research in toxicology, 11(7), 800-809 (1998-07-22)
The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography
K Kubo et al.
The Journal of antibiotics, 33(6), 556-565 (1980-06-01)
L-Amino acid acylase and D-amino acid acylase were stable below 50 degrees C, although the D-enzyme was more thermostable than the L-enzyme at higher temperatures. At 30 degrees C they showed the highest reaction velocity in phosphate buffer of pH
Debby Ngo et al.
JCI insight, 6(5) (2021-02-17)
Recent advances in proteomic technologies have made high-throughput profiling of low-abundance proteins in large epidemiological cohorts increasingly feasible. We investigated whether aptamer-based proteomic profiling could identify biomarkers associated with future development of type 2 diabetes (T2DM) beyond known risk factors.
Related Content
Global Trade Item Number
| SKU | GTIN |
|---|---|
| A3010-500MG | 04061832754529 |
| A3010-1G | 04061826680025 |
| A3010-100MG | 04061833360187 |
| A3010-5G | 04061832754536 |
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service