Western blot shows lysates of rat lung tissue. PVDF membrane was probed with 0.25 µg/mL of Goat Anti-Mouse/Rat MMP‑8 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3245) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for MMP‑8 at approximately 55 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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 (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, collagenase 2) 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 (1).
Tschesche, T. et al. (2004) Handbook of Proteolytic Enzymes (eds. A.J. Barrett et al.) p.480, Academic Press, San Diego.
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