Product nameRecombinant human MMP1 protein
See all MMP1 proteins and peptides
Protein lengthFull length protein
SourceHEK 293 cells
Amino Acid Sequence
Molecular weight52 kDa including tags
Amino acids1 to 469
TagsHis tag C-Terminus
Additional sequence informationMMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a polyhistide tag at the C-terminus.
Our Abpromise guarantee covers the use of ab124850 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
The activity was measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2. The specific activity is > 400 pmoles/min/µg.
Recombinant Human MMP-1 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
1. Dilute MMP1 to 50µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
2. Activate MMP1 by adding APMA to a final concentration of 1mM.
3. Incubate at 37°C for 2 hours.
Purity> 95 % SDS-PAGE.
ab124850 is purified by proprietary chromatographic techniques and 0.2µm sterile filtered.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.
Constituents: 25% MES, 25% Brij, 25% Glycerol, 25% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- 27 kDa interstitial collagenase
FunctionCleaves 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.
Sequence similaritiesBelongs to the peptidase M10A family.
Contains 4 hemopexin-like domains.
DomainThere 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.
modificationsUndergoes 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.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
ab124850 has not yet been referenced specifically in any publications.