| Reactivity | MuSpecies Glossary |
| Applications | ELISA(Cap), ELISA(Det) |
| Clone | 116134 |
| Clonality | Monoclonal |
| Host | Rat |
| Conjugate | Alexa Fluor 405 |
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Alexa Fluor 350 | FAB9092U-100UG | |||
| Alexa Fluor 488 | FAB9092G-100UG | |||
| Alexa Fluor 532 | FAB9092X-100UG | |||
| Alexa Fluor 594 | FAB9092T-100UG | |||
| Alexa Fluor 647 | FAB9092R-100UG | |||
| Alexa Fluor 700 | FAB9092N-100UG | |||
| Alexa Fluor 750 | FAB9092S-100UG | |||
| Unconjugated | MAB9092 | |||
| Immunogen | Mouse myeloma cell line NS0-derived recombinant mouse MMP‑9 Ala20-Pro730 Accession # P41245.1 |
| Specificity | Detects mouse Pro-MMP-9 in ELISAs. This antibody does not recognize the mature form of Pro-MMP-9. |
| Isotype | IgG2a |
| Clonality | Monoclonal |
| Host | Rat |
| Purity Statement | Protein A or G purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain. Compared to the human MMP-9 (Catalog # 911-MP), the mouse enzyme contains extra sequences in the linker region and in the hemopexin-like domain, respectively.
Secondary Antibodies |
Isotype Controls |
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