Analytical Data
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Gene name
MMP23B
- Application
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Alternative Names
MMP23B;MMP21;MMP22;Matrix metalloProteinase-23
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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
79-254aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSYTLTPARLRWDHFNLTYRILSFPRNLL SPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVS ALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDL VHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYG
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Molecular Weight
23 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
MMP23B, or Matrix Metalloproteinase 23B, is a member of the matrix metalloproteinase (MMP) family, which plays a crucial role in the degradation of extracellular matrix components. This protein is primarily implicated in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammation. Recent studies have highlighted the potential involvement of MMP23B in several diseases, such as cancer, arthritis, and cardiovascular disorders, due to its ability to regulate cellular environments and promote tumor invasion and metastasis. The understanding of MMP23B's function and mechanism of action has garnered interest in the scientific community, as it may serve as a biomarker for disease progression and a target for therapeutic interventions. Recombinant MMP23B protein is being produced for experimental studies aimed at elucidating its role in cellular dynamics and to explore its interactions with other extracellular matrix components and signaling pathways. Such research endeavors could pave the way for novel treatment strategies and enhance our knowledge of matrix biology in health and disease.
