Reactivity | MuSpecies Glossary |
Applications | ELISA(Cap) |
Clone | 116134 |
Clonality | Monoclonal |
Host | Rat |
Conjugate | Unconjugated |
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. |
Source | N/A |
Isotype | IgG2a |
Clonality | Monoclonal |
Host | Rat |
Gene | MMP9 |
Purity Statement | Protein A or G purified from hybridoma culture supernatant |
Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
Dilutions |
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Application Notes | ELISA Detection: Mouse Pro-MMP-9 Biotinylated Antibody (Catalog number BAM909) Standard: Recombinant Mouse MMP-9 (Catalog number 909-MM) |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
Preservative | No Preservative |
Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
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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