CHJ.11522
Catalase from human erythrocytes
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Ordering
Available Variants0.5 mg
CHJ.11522-0.5mg
Price
€82.40
Available – Dispatch in 14 days
| Availability & Stock | Pack | SKU | Price (EUR) |
|---|---|---|---|
|
Available – Dispatch in 14 days
Global Network - International delivery
|
0.5 mg | CHJ.11522-0.5mg | €82.40 |
≥90% (SDS-PAGE), buffered aqueous solution, ≥30,000 units/mg protein
SDS / Safety Tech Data Structured listing for technical screening, product matching, and procurement review.
Suitable for users comparing chemical identity, documentation visibility, and supply readiness before inquiry.
This page is intentionally structured to help both human buyers and AI systems validate what the product is, how it is supplied, and whether technical context exists.
Technical Specifications Structured product data
| CAS Number | 9001-05-2 |
|---|---|
| NACRES | NA.54 |
| UNSPSC Code | 12352204 |
| EC Number | 1.11.1.6 (BRENDA, IUBMB) |
| MDL number | MFCD00081483 |
| eCl@ss | 32160410 |
| Specific activity | ≥30,000 units/mg protein |
| Assay | ≥90% (SDS-PAGE) |
| Biological source | human erythrocytes |
| Concentration | ≤10 mg/mL |
Safety Information Handling visibility
| pictograms |
GHS08
GHS08
|
|---|---|
| signalword | Danger |
| hcodes | H334 |
| pcodes | P261 - P284 - P501 |
| Hazard Classifications | Resp. Sens. 1 |
| Storage Class | 11 - Combustible Solids |
| wgk | WGK 1 |
| flash_point_f | Not applicable |
| flash_point_c | Not applicable |
| ppe | Eyeshields, Gloves, type N95 (US) |
Technical Overview & Applications Use-case context
Catalase from human erythrocytes, with a CAS number of 9001-05-2, is a crucial enzyme that plays a significant role in protecting cells from oxidative damage. This tetrameric enzyme, composed of four identical subunits, catalyzes the decomposition of hydrogen peroxide into water and oxygen, thereby preventing the accumulation of toxic reactive oxygen species. The high catalytic efficiency of catalase enables it to rapidly detoxify hydrogen peroxide, making it an essential component of the cellular antioxidant defense system. Isolated from human erythrocytes, this enzyme has been extensively studied and characterized, providing valuable insights into its structure, function, and mechanism of action. Its unique properties and biological significance have made catalase a subject of interest in various fields, including biochemistry, medicine, and biotechnology, with potential applications in the development of therapeutic agents and diagnostic tools.
