Analytical Data
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Gene name
METTL11A
- Application
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Alternative Names
METTL11A；C9orf32；METTL11A；NRMT；N-terminal Xaa-Pro-Lys N-methyltransferase 1
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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
Q9BV86
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Expression Region
1-223aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFMTSEV IEDEKQFYSK AKTYWKQIPP TVDGMLGGYG HISSIDINSS RKFLQRFLRE GPNKTGTSCA LDCGAGIGRI TKRLLLPLFR EVDMVDITED FLVQAKTYLG EEGKRVRNYF CCGLQDFTPE PDSYDVIWIQ WVIGHLTDQH LAEFLRRCKG SLRPNGIIVI KDNMAQEGVI LDDVDSSVCR DLDVVRRIIC SAGLSLLAEE RQENLPDEIY HVYSFALR
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Molecular Weight
28 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
METTL11A is a recently identified member of the METTL (methyltransferase-like) protein family, which plays a crucial role in the post-translational modification of proteins, specifically through methylation processes. The protein has garnered attention due to its involvement in the regulation of cellular functions, including proliferation, differentiation, and stress responses. Preliminary studies suggest that METTL11A may influence various biological pathways, particularly in the context of oncogenesis and metabolic regulation. Given that aberrant methylation patterns are often associated with a range of diseases, including cancer, the study of METTL11A and its recombinant protein form is of significant interest for potential therapeutic interventions. Researchers aim to elucidate the enzymatic activity and substrate specificity of METTL11A through recombinant expression systems, which can facilitate functional assays and structural analyses. Understanding the molecular mechanisms underlying its action not only contributes to a broader comprehension of methylation's role in cellular homeostasis but also opens avenues for targeting METTL11A in disease states, potentially leading to innovative strategies for diagnosis and treatment. As such, the investigation of METTL11A recombinant proteins stands at the intersection of basic biological research and applied medical science, highlighting its relevance in both academic and clinical contexts.
