Human MMP-2 Antibody Summary
Accession # P08253
This antibody functions as an ELISA detection antibody when paired with Mouse Anti-Human MMP‑2 Monoclonal Antibody (Catalog # MAB9024).
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human MMP-2 DuoSet ELISA Kit (Catalog # DY902) for convenient development of a sandwich ELISA.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Human MMP‑2 ELISA Standard Curve. Recombinant Human MMP-2 protein was serially diluted 2-fold and captured by Mouse Anti-Human MMP-2 Monoclonal Antibody (Catalog # MAB9024) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human MMP-2 Monoclonal Antibody (Catalog # MAB9023) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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.
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