Analytical Data
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Gene name
YTHDF2
- Application
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Alternative Names
(DF2)(CLL-associated antigen KW-14)(High-glucose-regulated protein 8)(Renal carcinoma antigen NY-REN-2)
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Species
Human
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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
Q9Y5A9
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Expression Region
2-579aa
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Molecular Weight
68.2 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
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Protein Description
YTHDF2 is a member of the YTH domain family of proteins, which are recognized for their role in mRNA metabolism and regulation through the recognition of N6-methyladenosine (m6A) modifications. The presence of m6A modifications on mRNA molecules has been shown to influence various aspects of RNA biology, including stability, splicing, translation, and degradation. YTHDF2 specifically associates with m6A-modified mRNAs and is involved in the regulation of mRNA decay, thereby contributing to gene expression control. Research on YTHDF2 has gained momentum due to its implications in various biological processes and diseases, particularly in cancers, where altered m6A modification and dysregulation of RNA metabolism play critical roles. The recombinant expression of YTHDF2 has become a focal point of study, providing insight into its functions and interactions, as well as its potential as a therapeutic target. Understanding the structural and functional characteristics of YTHDF2 through recombinant protein studies can help elucidate its mechanisms of action and pave the way for novel strategies in treating diseases associated with m6A dysregulation.
