Analytical Data
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Gene name
MMP3
- Application
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Alternative Names
MMP3;STMY1;Stromelysin-1
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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
P08254
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Expression Region
101-477aa
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AA Sequence
MRTFPGIPKW RKTHLTYRIV NYTPDLPKDA VDSAVEKALK VWEEVTPLTF SRLYEGEADI MISFAVREHG DFYPFDGPGN VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE IGHSLGLFHS ANTEALMYPL YHSLTDLTRF RLSQDDINGI QSLYGPPPDS PETPLVPTEP VPPEPGTPAN CDPALSFDAV STLRGEILIF KDRHFWRKSL RKLEPELHLI SSFWPSLPSG VDAAYEVTSK DLVFIFKGNQ FWAIRGNEVR AGYPRGIHTL GFPPTVRKID AAISDKEKNK TYFFVEDKYW RFDEKRNSME PGFPKQIAED FPGIDSKIDA VFEEFGFFYF FTGSSQLEFD PNAKKVTHTL KSNSWLNC
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Molecular Weight
43 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
Matrix metalloproteinase-3 (MMP-3), also known as stromelysin-1, is an enzyme that plays a critical role in the degradation of extracellular matrix (ECM) components, which is essential for tissue remodeling, repair, and development. Dysfunctional regulation of MMP-3 has been implicated in various pathological conditions, including arthritis, cancer metastasis, and cardiovascular diseases. Understanding the structure-function relationship of MMP-3 is crucial for developing therapeutic interventions. Recombinant expression of MMP-3 allows researchers to produce this enzyme in a controlled environment, facilitating the study of its biochemical properties, substrate specificity, and inhibition. Furthermore, the generation of MMP-3 as a recombinant protein enables high-throughput screening for novel inhibitors, which could serve as potential therapeutic agents in diseases characterized by excessive ECM degradation. The production of MMP-3 in heterologous systems, such as bacteria or yeast, thus represents a valuable tool in biomedical research, providing insights into its role in health and disease and advancing the development of targeted treatments aiming to manipulate its activity.
