Analytical Data
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Gene name
MMP11
- Application
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Alternative Names
MMP11；STMY3；Stromelysin-3
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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
P24347
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Expression Region
98-488aa
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AA Sequence
FVL SGGRWEKTDL TYRILRFPWQ LVQEQVRQTM AEALKVWSDV TPLTFTEVHE GRADIMIDFA RYWHGDDLPF DGPGGILAHA FFPKTHREGD VHFDYDETWT IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR YPLSLSPDDC RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA QGHIWFFQGA QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI YFFRGRDYWR FHPSTRRVDS PVPRRATDWR GVPSEIDAAF QDADGYAYFL RGRLYWKFDP VKVKALEGFP RLVGPDFFGC AEPANTFL
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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
MMP11, also known as stromelysin-3, is a member of the matrix metalloproteinase (MMP) family, which plays a crucial role in the remodeling of extracellular matrix (ECM) components. It is mainly expressed in various tissues during embryonic development and in pathological conditions such as cancer, where it is implicated in tumor progression, invasion, and metastasis. The increased expression of MMP11 has been associated with poor prognosis in several malignancies, making it a target of interest for therapeutic interventions. Research on MMP11 recombinant proteins has gained traction in recent years, aiming to elucidate its precise functions and regulatory mechanisms in normal and diseased states. By producing MMP11 as a recombinant protein, scientists can explore its enzymatic activity, identify potential substrates, and examine its role in ECM degradation. Additionally, understanding the structure-function relationship of MMP11 can facilitate the development of specific inhibitors for cancer treatment and other disorders involving ECM dysregulation. Overall, the study of MMP11 and its recombinant protein forms holds significant potential for advancing our knowledge of ECM dynamics and contributing to novel therapeutic strategies against cancer and other diseases.
