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Human TRMT112 Recombinant Protein (C-Strep) (HC763012)

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Overview
Catalog No.HC763012
Description
Recombinant Human TRMT112 Protein, C-Strep (HC763012) expressed in E. coli, spanning Met1-Ser125. Purity: >90% by SDS-PAGE.
Highlights
  • E. coli Expression — High-yield, cost-effective production.
  • High Purity — >90% purity verified by SDS-PAGE.
Expression systemE. coli
AccessionQ9UI30
Protein lengthMet1-Ser125
ApplicationsELISA, Immunogen, SDS-PAGE, WB, Bioactivity testing in progress
SpeciesHomo sapiens (Human)
Nature Recombinant
Endotoxin level Please contact with the lab for this information.
Purity >90% as determined by SDS-PAGE.
Predicted molecular weight 15.37 kDa
Form Lyophilized
Storage buffer Lyophilized from a solution in PBS pH 7.4, 1 mM EDTA, 4% Trehalose, 1% Mannitol.

Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.

Reconstitution Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Shipping In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise.
Stability and Storage Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Alternate NamesMultifunctional methyltransferase subunit TRM112-like protein, TRMT112, tRNA methyltransferase 112 homolog
Background

Multifunctional methyltransferase subunit TRM112-like protein is a ~14 kDa protein. Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with N6AMT1/HEMK2 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with N6AMT1/HEMK2 also monomethylates 'Lys-12' of histone H4 (H4K12me1). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species.

1. Figaro, S. et al. (2008) FEBS letters 582, 2352-6. PMID: 18539146
2. Fu, D. et al. (2010) Molecular and cellular biology 30, 2449-59. PMID: 20308323
3. Zorbas, C. et al. (2015) Molecular biology of the cell 26, 2080-95. PMID: 25851604
4. Metzger, E. et al. (2019) Nature structural & molecular biology 26, 361-371. PMID: 31061526
5. van Tran, N. et al. (2019) Nucleic acids research 47, 7719-7733. PMID: 31328227
6. Li, W. et al. (2019) Cell discovery 5, 51. PMID: 31636962
7. Wang, C. et al. (2023) Nucleic acids research 51, 7496-7519. PMID: 37283053
9. Yu, D. et al. (2021) The Journal of biological chemistry 296, 100270. PMID: 33428944
10. Sepich-Poore, C. et al. (2022) The Journal of biological chemistry 298, 101590. PMID: 35033535
Note For research use only
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Formula
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Formula
C₁ × V₁ = C₂ × V₂
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