Analytical Data
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Gene name
METTL14
- Application
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Alternative Names
Methyltransferase-like protein 14;hMETTL14
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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
Q9HCE5
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Expression Region
1-456 aa
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AA Sequence
MDSRLQEIRERQKLRRQLLAQQLGAESADSIGAVLNSKDEQREIAETRETCRASYDTSAPNAKRKYLDEGETDEDKMEEYKDELEMQQDEENLPYEEEIYKDSSTFLKGTQSLNPHNDYCQHFVDTGHRPQNFIRDVGLADRFEEYPKLRELIRLKDELIAKSNTPPMYLQADIEAFDIRELTPKFDVILLEPPLEEYYRETGITANEKCWTWDDIMKLEIDEIAAPRSFIFLWCGSGEGLDLGRVCLRKWGYRRCEDICWIKTNKNNPGKTKTLDPKAVFQRTKEHCLMGIKGTVKRSTDGDFIHANVDIDLIITEEPEIGNIEKPVEIFHIIEHFCLGRRRLHLFGRDSTIRPGWLTVGPTLTNSNYNAETYASYFSAPNSYLTGCTEEIERLRPKSPPPKSKSDRGGGAPRGGGRGGTSAGRGRERNRSNFRGERGGFRGGRGGAHRGGFPPR
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Molecular Weight
59.2 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
METTL14, a vital component of the N6-methyladenosine (m6A) methyltransferase complex, plays a significant role in RNA methylation, impacting various biological processes such as gene expression regulation, RNA stability, and splicing. The m6A modification has emerged as a crucial player in cellular functions and has been implicated in diverse physiological and pathological contexts, including development, immunity, and cancer. Understanding METTL14's structure and function is essential for elucidating the molecular mechanisms underlying m6A modification and its downstream effects on gene regulation. Recent studies have highlighted METTL14's involvement in modulating RNA methylation patterns and its potential as a therapeutic target in diseases associated with dysregulated m6A signaling. Research on recombinant METTL14 protein aims to explore its enzymatic activity, binding affinities, and interactions with RNA and other protein partners. This knowledge will enhance our understanding of the m6A methylation landscape and contribute to the development of novel strategies for therapeutic interventions in conditions linked to METTL14 dysfunction, paving the way for advancements in RNA biology and medicine.
