Analytical Data
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Gene name
METTL17
- Application
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Alternative Names
False p73 target gene protein;Methyltransferase 11 domain-containing protein 1;Protein RSM22 homolog, mitochondrial
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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
Q9H7H0
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Expression Region
20-456 aa
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AA Sequence
VAPQARALAALVPGVTQVDNKSGFLQKRPHRQHPGILKLPHVRLPQALANGAQLLLLGSAGPTMENQVQTLTSYLWSRHLPVEPEELQRRARHLEKKFLENPDLSQTEEKLRGAVLHALRKTTYHWQELSYTEGLSLVYMAARLDGGFAAVSRAFHEIRARNPAFQPQTLMDFGSGTGSVTWAAHSIWGQSLREYMCVDRSAAMLVLAEKLLKGGSESGEPYIPGVFFRQFLPVSPKVQFDVVVSAFSLSELPSKADRTEVVQTLWRKTGHFLVLVENGTKAGHSLLMDARDLVLKGKEKSPLDPRPGFVFAPCPHELPCPQLTNLACSFSQAYHPIPFSWNKKPKEEKFSMVILARGSPEEAHRWPRITQPVLKRPRHVHCHLCCPDGHMQHAVLTARRHGRDLYRCARVSSWGDLLPVLTPSAFPPSTAQDPSES
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Molecular Weight
54.8 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
METTL17, a member of the methyltransferase-like family, has garnered significant interest in recent years due to its role in cellular processes such as RNA methylation and regulation of gene expression. This protein is known to modify adenosine residues in RNA, influencing stability and translation efficiency, which can have profound implications for cellular function and organismal development. Research indicates that aberrant METTL17 activity may be linked to various diseases, including cancer and neurodegenerative disorders, underscoring the need for detailed studies on its mechanism of action. To facilitate these investigations, the production of recombinant METTL17 proteins is crucial. This enables researchers to obtain pure and functional protein for in vitro studies and structural analysis. These studies can provide insights into the enzymatic properties of METTL17, identify potential interacting partners, and elucidate its biological pathways. Moreover, understanding the precise role of METTL17 in RNA modification could open avenues for therapeutic interventions aimed at diseases associated with its dysregulation. As a result, the characterization of recombinant METTL17 is a pivotal step in advancing our knowledge of its functions and therapeutic potential in the context of health and disease.
