Analytical Data
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Gene name
MMP7
- Application
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Alternative Names
MMP7；MPSL1；PUMP1；Matrilysin
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09237
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Expression Region
1~267aa
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AA Sequence
LPLPQEAGGMSELQWEQAQDYLKRFYLYDSETKNANSLEAKLKEMQKFFG LPITGMLNSRVIEIMQKPRCGVPDVAEYSLFPNSPKWTSKVVTYRIVSYT RDLPHITVDRLVSKALNMWGKEIPLHFRKVVWGTADIMIGFARGAHGDSY PFDGPGNTLAHAFAPGTGLGGDAHFDEDERWTDGSSLGINFLYAATHELG HSLGMGHSSDPNAVMYPTYGNGDPQNFKLSQDDIKGIQKLYGKRSNS
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Molecular Weight
33kDa
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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
Identification
Protein Description
MMP7, or Matrix Metalloproteinase-7, is an essential enzyme that plays a critical role in extracellular matrix remodeling and tissue homeostasis. It belongs to the MMP family, which is involved in various physiological and pathological processes, including wound healing, inflammation, and cancer progression. The dysregulation of MMP7 activity has been implicated in several diseases, particularly in cancer metastasis, where it facilitates tumor invasion and migration by degrading extracellular matrix components. Given its significance in disease mechanisms, the recombinant expression of MMP7 has garnered substantial interest in research. Producing MMP7 as a recombinant protein allows for a detailed study of its enzymatic activity, function, and interactions with other biomolecules in vitro and in vivo. Additionally, the availability of purified MMP7 can aid in the development of therapeutic agents and diagnostic tools targeting MMP-related pathologies. Understanding MMP7's structure-function relationship and its role in various biological contexts may pave the way for innovative strategies in disease management and treatment. Thus, research on recombinant MMP7 not only addresses fundamental biological questions but also holds promise for translational applications in medicine.
