Reactivity | HuSpecies Glossary |
Applications | WB |
Clonality | Polyclonal |
Host | Goat |
Conjugate | Biotin |
Concentration | LYOPH |
Immunogen | Chinese hamster ovary cell line CHO-derived recombinant human MMP‑2 (R&D Systems, Catalog # 902-MP) Ile34-Cys660 Accession # P08253 |
Specificity | Detects pro/active human MMP-2 in Western blots. In this format, approximately 50% cross-reactivity with recombinant mouse MMP‑2 is observed and less than 1% cross-reactivity with recombinant human (rh) MMP-1, rhMMP-3, rhMMP-8, rhMMP-9, rhMMP-10, rhMMP-12, and rhMMP-13 is observed. |
Source | N/A |
Isotype | IgG |
Clonality | Polyclonal |
Host | Goat |
Gene | MMP2 |
Purity Statement | Antigen Affinity-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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Readout System | ||
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 BSA as a carrier protein. |
Preservative | No Preservative |
Concentration | LYOPH |
Reconstitution Instructions | Reconstitute at 0.2 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-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. 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-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites.
Secondary Antibodies |
Isotype Controls |
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