Analytical Data
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Gene name
MEC
- Application
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Alternative Names
MEC；Methyl-CpG-binding Protein 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
Q9NRJ3-1
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Expression Region
20-127aa
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AA Sequence
SEAILPIASSCCTEVSHHISRRLLERVNMCRIQRADGDCDLAAVILHVKR RRICVSPHNHTVKQWMKVQAAKKNGKGNVC HRKKHHGKRNSNRAHQGKHETYGHKTPY
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Molecular Weight
12 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
MEC (Mucin Excising Complex) recombinant proteins have garnered significant attention in recent years due to their potential applications in biomedical research and therapeutic development. Initially identified for their roles in cellular adhesion and signaling, mucins are glycoproteins that play crucial roles in maintaining mucosal barriers and facilitating cell communication. The study of MEC recombinant proteins is critical for understanding the pathology of various diseases, including cancer and inflammatory conditions, where altered mucin expression or function is observed. Advances in molecular biology techniques have enabled the efficient production and characterization of these proteins, allowing researchers to investigate their structure-function relationships and interactions with other cellular components. Furthermore, MEC recombinant proteins serve as valuable tools for developing diagnostic markers and therapeutic agents, leveraging their ability to modulate immune responses and influence tumor progression. The growing interest in personalized medicine and targeted therapies further underscores the need for comprehensive studies on MEC recombinant proteins, paving the way for innovative strategies in disease management and treatment. As the field evolves, collaboration among researchers, clinicians, and biopharmaceutical companies will be essential to translate these findings into practical applications.
