Analytical Data
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Gene name
MMP17
- Application
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Alternative Names
MMP17；MT4MMP；Matrix metalloProteinase-17
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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
Q9ULZ9
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Expression Region
126-565aa
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AA Sequence
QAPAP TKWNKRNLSW RVRTFPRDSP LGHDTVRALM YYALKVWSDI APLNFHEVAG SAADIQIDFS KADHNDGYPF DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM DLFAVAVHEF GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK GKYFWRLTRD RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF KGDRYWVFKD NNVEEGYPRP VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD DAMRWSDGAS YFFRGQEYWK VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE GPRAPPGQHD QSRSEDGYEV CSCTS
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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
MMP17, also known as Membrane Type 17 Matrix Metalloproteinase (MT-MMP), is an important member of the matrix metalloproteinase (MMP) family, which is known for its role in extracellular matrix (ECM) remodeling. The research on MMP17 has gained attention due to its involvement in various physiological and pathological processes, including tissue remodeling, wound healing, and cancer metastasis. Unlike other MMPs that are secreted, MMP17 is anchored to the cell membrane, allowing it to interact directly with the ECM and neighboring cells. This unique localization suggests that MMP17 may play a critical role in regulating cell-matrix interactions and signal transduction pathways. Elevated expression levels of MMP17 have been implicated in aggressive tumor phenotypes and poor prognosis in cancer patients, making it a potential biomarker and therapeutic target. Furthermore, MMP17 is believed to participate in the activation of other MMPs, forming a complex regulatory network that influences ECM dynamics. With advancements in recombinant protein technology, the production and characterization of MMP17 recombinant proteins have become feasible, providing valuable tools for studying its enzymatic activity, substrate specificity, and physiological roles. Understanding the mechanisms underlying MMP17-mediated processes could pave the way for novel therapeutic strategies in treating diseases where ECM remodeling plays a crucial role, such as fibrosis and cancer. Therefore, investigating MMP17 in detail represents a promising avenue for both basic research and clinical applications in the fields of oncology and regenerative medicine.
