A5147
L-Amino Acid Oxidase from Crotalus atrox (Western Diamondback Rattlesnake)
Type VI, dried venom
Synonym(s):
L-AAO, L-Amino acid: oxygen oxidoreductase (deaminating)
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-564-0
MDL number:
Product Name
L-Amino Acid Oxidase from Crotalus atrox (Western Diamondback Rattlesnake), Type VI, dried venom
type
Type VI
form
dried venom
storage temp.
−20°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
Application
L-amino acid oxidase is used to convert L-amino acids to their corresponding α-keto acids. Product A5147 is from Crotalus atrox. L-amino acid oxidase, from Sigma, has been used in leucine aminopeptidase (LAP) activity assays .
Biochem/physiol Actions
L-amino acid oxidase is involved in various metabolic pathways such as alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis .
signalword
Danger
hcodes
Hazard Classifications
Acute Tox. 1 Inhalation - Acute Tox. 2 Dermal - Acute Tox. 2 Oral
Storage Class
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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.
Saad Alrashdi et al.
Molecules (Basel, Switzerland), 28(1) (2023-01-09)
Indole-containing acyloins are either key intermediates of many antimicrobial/antiviral natural products or building blocks in the synthesis of biologically active molecules. As such, access to structurally diverse indole-containing acyloins has attracted considerable attention. In this report, we present a pilot
Jiro Arima et al.
The Journal of biological chemistry, 281(9), 5885-5894 (2006-01-13)
Streptomyces griseus leucine aminopeptidase (SGAP), which has two zinc atoms in its active site, is clinically important as a model for understanding the structure and mechanism of action of other metallopeptidases. SGAP is a calcium-activated and calcium-stabilized enzyme, and its
Anwar Ullah et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 68(Pt 2), 211-213 (2012-02-03)
Snake-venom L-amino-acid oxidases (SV-LAAOs) trigger a wide range of local and systematic effects, including inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. These effects mainly arise from the uncontrolled release of the hydrogen peroxide that is produced by the
Zhiliang Yu et al.
Applied biochemistry and biotechnology, 167(1), 1-13 (2012-03-01)
L-amino acid oxidase is widely found in diverse organisms and has different properties. It is thought to contribute to antimicrobial activity, amino acid catabolism, and so forth. The purpose of this communication is to summarize the advances in non-snake venom
Chi-Hua Cheng et al.
Analytical biochemistry, 420(1), 93-95 (2011-09-29)
As opposed to single-cell yeast and mammalian cell lines, apoptosis has not been greatly investigated in filamentous fungi because antibodies to the relevant fungal apoptosis-related proteins are not available commercially and because multicellular organisms cannot be studied using flow cytometry.
Related Content
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