Analytical Data
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Gene name
MMP14
- Application
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Alternative Names
MMP14;Matrix metalloProteinase-14
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50281
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Expression Region
112-288aa
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AA Sequence
YAIQGLKWQHN EITFCIQNYT PKVGEYATYE AIRKAFRVWE SATPLRFREV PYAYIREGHE KQADIMIFFA EGFHGDSTPF DGEGGFLAHA YFPGPNIGGD THFDSAEPWT VRNEDLNGND IFLVAVHELG HALGLEHSSD PSAIMAPFYQ WMDTENFVLP DDDRRGIQQL YGGESG
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Molecular Weight
20 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
MMP14, also known as membrane-type matrix metalloproteinase 1 (MT1-MMP), is a crucial enzyme involved in the degradation of extracellular matrix components, playing a pivotal role in various biological processes such as tissue remodeling, wound healing, and invasion of cancer cells. Its activity is tightly regulated, as abnormal MMP14 expression and function have been associated with various pathologies, including cancer metastasis, cardiovascular diseases, and inflammatory disorders. The interest in studying MMP14 has surged due to its potential as a therapeutic target; thus, the development of recombinant MMP14 proteins is essential for advancing our understanding of its biochemical properties and roles in disease progression. Recombinant MMP14 not only facilitates the investigation into its catalytic mechanism and substrate specificity but also enables the screening of MMP14 inhibitors, which could pave the way for novel therapeutic strategies. Furthermore, insights gained from recombinant MMP14 research could lead to the identification of biomarkers for disease diagnosis and prognosis, as well as enhancing the development of MMP-related biopharmaceuticals. Overall, the study of MMP14 through recombinant protein technology offers a promising avenue for unraveling its complex functions in health and disease.
