| Reactivity | HuSpecies Glossary |
| Applications | WB, IP, ELISA(Cap), ELISA(Det) |
| Clone | 100619 |
| Clonality | Monoclonal |
| Host | Mouse |
| Conjugate | Alexa Fluor 488 |
| Immunogen | Mouse myeloma cell line NS0-derived recombinant human MMP‑8 Phe21-Gly467 Accession # AAZ38714 |
| Specificity | Detects the pro and active forms of human MMP-8 in Western blots. Does not cross-react with recombinant human (rh) MMP‑1, -2, -3, -7, -9, -10, -12, or -13. |
| Isotype | IgG2b |
| Clonality | Monoclonal |
| Host | Mouse |
| 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. |
| Dilutions |
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| 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 (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP‑8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP‑8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP‑8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis,
MMP‑8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP‑8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain. MMP‑8 is heavily glycosylated.
Secondary Antibodies |
Isotype Controls |
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