Recombinant human MMP14 protein (Active) (ab157068)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: Functional Studies, SDS-PAGE
Description
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Product name
Recombinant human MMP14 protein (Active)
See all MMP14 proteins and peptides -
Biological activity
≥140mU/mg protein.
One unit is defined as the amount of enzyme that hydrolyzes 1µmol Mca-Pro-LeuGly-Leu-Dpa-Ala-Arg-NH2 per min. at 37°C, pH 7.5
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Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
YAIQGLKWQHN EITFCIQNYT PKVGEYATYE AIRKAFRVWE SATPLRFREV PYAYIREGHE KQADIMIFFA EGFHGDSTPF DGEGGFLAHA YFPGPNIGGD THFDSAEPWT VRNEDLNGND IFLVAVHELG HALGLEHSSD PSAIMAPFYQ WMDTENFVLP DDDRRGIQQL YGGESG -
Predicted molecular weight
20 kDa -
Amino acids
112 to 288
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Specifications
Our Abpromise guarantee covers the use of ab157068 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Functional Studies
SDS-PAGE
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Form
Liquid -
Additional notes
Inhibitors: The catalytic domain of MMP-14 is inhibited by tissue inhibitors of MMP-2 and -3 (TIMP-2 and TIMP-3) and by chelators of divalent cations like EDTA or o-phenanthroline.
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Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on Dry Ice. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.06% Calcium chloride, 0.79% Tris HCl, 0.87% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
General Info
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Alternative names
- Matrix metallopeptidase 14 (membrane inserted)
- Matrix metalloproteinase 14
- Matrix metalloproteinase-14
see all -
Function
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. -
Tissue specificity
Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors. -
Sequence similarities
Belongs to the peptidase M10A family.
Contains 4 hemopexin-like domains. -
Domain
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. -
Post-translational
modificationsThe precursor is cleaved by a furin endopeptidase. -
Cellular localization
Membrane. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. - Information by UniProt
Protocols
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.
Datasheets and documents
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Datasheet download
References (0)
ab157068 has not yet been referenced specifically in any publications.