Analytical Data
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Gene name
MYDGF
- Application
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Alternative Names
SF20; IL25; IL27w; C19orf10; Interleukin 27 Working Designation; Interleukin-25; Stromal cell-derived growth factor SF20
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Species
Mouse
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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
Q9CPT4
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Expression Region
Val25~Leu166
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Molecular Weight
23kDa
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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
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Protein Description
MYDGF, or Myeloid-Derived Growth Factor, is a protein that has garnered significant attention in the fields of immunology and cancer research due to its role in modulating cell growth, differentiation, and immune responses. Emerging studies suggest that MYDGF plays a crucial part in the tumor microenvironment, particularly in how myeloid cells influence tumor progression and the immune landscape. Research indicates that MYDGF can promote tumor cell survival and proliferation while potentially suppressing effective anti-tumor immune responses. The understanding of MYDGF's mechanisms of action is essential for developing targeted therapies aimed at improving cancer treatment outcomes. Moreover, MYDGF has been implicated in various inflammatory diseases, highlighting its potential as a therapeutic target beyond oncology. The exploration of MYDGF's structure, function, and pathways is key in elucidating its diverse biological roles and developing novel strategies for intervention in diseases characterized by abnormal cell growth and inflammation. As such, the study of MYDGF and its recombinant forms holds promise for advancing our understanding of complex disease mechanisms and identifying new avenues for therapeutic development.
