The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/1000 - 1/5000. Detects a band of approximately 51, 53 kDa (predicted molecular weight: 54 kDa). A recommended starting concentration for Western blots is 1/1000 when using colorimetric substrates such as BCIP/NBT and 1/5000 for chemiluminescent substrates. Collagenase levels in quiescent cells and tissues is minimal, and stimulation of protein concentration is often needed to visualize the bands.
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases). The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.
Secreted > extracellular space > extracellular matrix.
References for Anti-MMP1 antibody [3A9.3] (ab38923)
This product has been referenced in:
Pozgan U et al. Expression and activity profiling of selected cysteine cathepsins and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis. Biol Chem391:571-9 (2010).
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