Key features and details
- Expression system: Native
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
Product nameNative human MMP1 protein
See all MMP1 proteins and peptides
Biological activityThe specific activity of ab134442 is >100 mU/mg when assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly Ile-Ala-Gly-Gln-D-Arg (Dnp-petide).
Purity> 90 % SDS-PAGE.
Protein lengthFull length protein
Amino acids1 to 469
Our Abpromise guarantee covers the use of ab134442 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Additional notesDo not dilute ab134442 for activation. The enzyme needs to be activated by trypsin (2 µl trypsin; 1mg/ml) for 10 - 20 min. at 37°C and stopped by the addition of inhibitor (10 µl trypsin-inhibitor; 2 mg/ml or aprotinin or TLCK) or activation by 2 mM (final concentration) aminophenylmercuric acetate (APMA, FW 351.8) for 60 min at 37°C.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Preservative: 0.05% Sodium azide
Constituents: 0.05% Brij, 0.05% Calcium chloride, 0.001% Zinc chloride, 0.79% Tris HCl, 1.75% 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
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab134442 has not yet been referenced specifically in any publications.