56177
Hyaluronate Lyase from Streptococcus pyogenes
≥8.0 units/mg protein (5.0-15.0 mg/mL)
Synonym(s):
Hyaluronidase from Streptococcus pyogenes
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About This Item
Specific activity:
≥8.0 units/mg protein (5.0-15.0 mg/mL)
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
liquid
specific activity
≥8.0 units/mg protein (5.0-15.0 mg/mL)
storage temp.
2-8°C
Biochem/physiol Actions
Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. It is important for the diffusion of toxins and proteins produced by S. pyogenes.
Hyaluronate lyase degrades hyaluronate using an elimination reaction to break glycosidic linkages yielding unsaturated disaccharide products. It is important for the diffusion of toxins and proteins produced by S. pyogenes.
Physical form
ammonium sulfate suspension
Other Notes
1 U corresponds to the amount of enzyme which liberates 1 μmol unsaturated disaccharides per minute at pH 6.0 and 37°C from hyaluronic acid (Product No. 53747).
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Structural studies on the bacterial lyase-resistant tetrasaccharides derived from the antithrombin III-binding site of porcine intestinal heparin.
Yamada, S., et al.
The Journal of Biological Chemistry, 4780-4787 (1993)
R J Linhardt et al.
Applied biochemistry and biotechnology, 12(2), 135-176 (1986-04-01)
Polysaccharide lyases (or eliminases) are a class of enzymes (EC 4.2.2.-) that act to cleave certain activated glycosidic linkages present in acidic polysaccharides. These enzymes act through an eliminase mechanism, rather than through hydrolysis, resulting in unsaturated oligosaccharide products. Acidic
Substrate specificity of the heparin lyases from Flavobacterium heparinum.
Desai, U.R., et al.
Archives of Biochemistry and Biophysics, 461-468 (1993)
M J Jedrzejas
Cellular and molecular life sciences : CMLS, 64(21), 2799-2822 (2007-08-10)
Bacteria present a variety of molecules either on their surface or in a cell-free form. These molecules take part in numerous processes in the interactions with their host, with its tissues and other molecules. These molecules are essential to bacterial
Md Sohail Akhtar et al.
Biochemical and biophysical research communications, 353(2), 286-292 (2006-12-26)
Hyaluronate lyases from Streptococcus pneumoniae (SpnHL) and Streptococcus agalactiae (SagHL) are composed of four domains; N-terminal domain, spacer domain, alpha-domain and C-terminal domain, which are connected through peptide linkers. We have earlier shown that the recombinant alpha- and C-terminal domains
Global Trade Item Number
| SKU | GTIN |
|---|---|
| P162-100MG | 04061834355908 |
| P162-25MG | 04061832083612 |
| 8028340100 | 04022536768731 |
| 8028340025 | 04022536376561 |
| 30050-25G-F | 04061826658949 |
| C8707-25G | 04061833610336 |
| 30050-100G-F | 04061826658871 |
| 02712-100G | 04061832607467 |
| 02712-750G | 04061832607474 |
| C8707-100G | 04061833619186 |
| C121509-500G | 04061832884622 |
| C121509-25G | 04061833461846 |
| C121509-100G | 04061833461839 |
| 56177-50MG | 04061833228166 |
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