Analytical Data
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Gene name
MMP23A
- Application
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Alternative Names
MMP23A；
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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
O75900
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Expression Region
1-390aa
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AA Sequence
MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSA AQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSF PRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHT DCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGV WLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLH RLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATT PPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLA LGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG
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Molecular Weight
43.9 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
MMP23A, a member of the matrix metalloproteinase (MMP) family, plays a crucial role in the remodeling of extracellular matrix components and is implicated in various physiological processes, including embryogenesis, wound healing, and tissue repair. Research has increasingly focused on MMP23A due to its potential involvement in pathological conditions such as cancer metastasis, fibrosis, and inflammatory diseases. Understanding the functionality of MMP23A is essential, as its dysregulation can lead to enhanced tissue degradation and contribute to disease progression. Recombinant MMP23A protein has been produced to facilitate in-depth studies of its enzymatic activity, substrate specificity, and regulatory mechanisms. These studies typically employ techniques such as zymography and enzyme assays to analyze its functional properties. Moreover, the development of MMP23A inhibitors may provide novel therapeutic strategies for diseases characterized by excessive matrix degradation. Consequently, research on recombinant MMP23A not only furthers our understanding of its biological roles but also holds promise for developing targeted therapies that could ameliorate diseases associated with MMP dysregulation.
