Myeloperoxidase Human Protein
Specifications
| Product Data | |
| Species | Human |
|---|---|
| Protein Source | Leukocytes |
| Concentration | lot specific |
| Purity | >95% pure (SDS-PAGE) by Column Chromatography |
| Presentation State | Purified |
| Buffer | Presentation State: Purified State: Lyophilized Buffer System: 50 mM Sodium Acetate, pH 6.0 containing 100 mM Sodium Chloride |
| Bioactivity | Specific: >200 units per mg protein after lyophilization. One unit is defined as the amount of enzyme that will decompose 1.0 micromole of hydrogen peroxide per minute at 25°C, pH 6.0. |
| Reconstitution Method | Reconstitute with distilled water |
| Preparation | Lyophilized |
| Protein Description | Human Neutrophil Myeloperoxidase. |
| Note | Caution: All human source materials have tested negative for HIV 1 and HIV2 antibodies and non-reactive for HCV and HBc antibodies and HBsAg. No test guarantees a product to be non-infectious. Therefore, all material derived from human fluids or tissues should be considered as potentially infectous. |
| Storage | Store at -20°C. Avoid repeated freezing and thawing. |
| Stability | Shelf life: Six months from despatch. |
| Shipping | Ambient |
| Reference Data | |
| RefSeq | NP_000241 |
| Locus ID | 4353 |
| Cytogenetics | 17q22 |
| Synonyms | MPO |
| Summary | Myeloperoxidase (MPO) is a heme protein synthesized during myeloid differentiation that constitutes the major component of neutrophil azurophilic granules. Produced as a single chain precursor, myeloperoxidase is subsequently cleaved into a light and heavy chain. The mature myeloperoxidase is a tetramer composed of 2 light chains and 2 heavy chains. This enzyme produces hypohalous acids central to the microbicidal activity of neutrophils. provided by RefSeq, Nov 2014 |
| Protein Categories | Immune system diseases, Intracellular Proteins |
| Protein Families | Druggable Genome |
Reviews
Documents
| FAQs |
| SDS |
Resources
| Recombinant Protein Resources |
Citations
Esposito, Kontra, Giacomassi et al
Front Immunol (2023) 14, 1164941 DOI: 10.3389/fimmu.2023.1164941
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