Analytical Data
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Gene name
MMP23A
- Application
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Alternative Names
CA-MMP; MMP23-A; MIFR; MIFR-1; MMP-21; Pseudogene; Femalysin; Matrix metalloproteinase-23, soluble form
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O88272
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Expression Region
Ser71~Tyr383
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Molecular Weight
40kDa
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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, is an enzyme known to play a significant role in extracellular matrix remodeling and tissue repair processes. Initially identified in the context of pathological conditions, such as cancer and inflammation, MMP23A is believed to contribute to the degradation of various extracellular matrix components, thereby influencing cellular behavior, migration, and invasion. Research has shown that MMP23A is involved in key biological processes, including wound healing, angiogenesis, and tumor progression, making it a potential target for therapeutic interventions. Additionally, its unique expression patterns and regulatory mechanisms have garnered attention in the field of regenerative medicine, where understanding its function could lead to novel strategies for tissue regeneration. The production of recombinant MMP23A protein is crucial for elucidating its biological functions, interactions, and potential as a biomarker for disease progression or therapeutic response. Thus, ongoing studies aim to characterize the biochemical properties and regulatory pathways of MMP23A, facilitating the development of MMP-targeted therapies and enhancing our understanding of its role in health and disease.
