Analytical Data
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Gene name
MMP10
- Application
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Alternative Names
MMP10;STMY2;Stromelysin-2
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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
P09238
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Expression Region
99-476aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSFSSFPGMPKWRKTHLTYRIVNYTPDLP RDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDG PGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGL FHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVP TKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEF HLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGI HTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLI ADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLH C
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Molecular Weight
45 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 10 (MMP10), also known as stromelysin-2, is a member of the matrix metalloproteinase family, which plays a crucial role in extracellular matrix remodeling. This enzyme is involved in various physiological processes, including tissue repair, cell migration, and apoptosis, as well as pathological conditions such as cancer metastasis, cardiovascular diseases, and inflammatory disorders. Research on MMP10 has intensified due to its significant implications in disease mechanisms and potential therapeutic targets. Understanding the structure-function relationship of MMP10 and its regulatory mechanisms can provide insights into its role in disease progression. Additionally, its expression is modulated by various cytokines and growth factors, which underscores its complexity in biological processes. The study of recombinant MMP10 proteins has facilitated the investigation of its enzymatic activity, substrate specificity, and interaction with inhibitors. This research is essential for developing novel therapeutic strategies, leveraging MMP10 as a biomarker for disease states, and designing specific inhibitors that could potentially mitigate the adverse effects associated with its overexpression. Furthermore, MMP10's role in the tumor microenvironment emphasizes the need for thorough exploration of its functions in cancer biology. Overall, ongoing studies of recombinant MMP10 proteins not only enhance the understanding of its biological significance but also pave the way for innovative approaches in treating diseases linked to abnormal MMP activity.
