Analytical Data
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Gene name
BHMT2
- Application
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Alternative Names
BHMT2；S-methylmethionine--homocysteine S-methyltransferase BHMT2
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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
Q9H2M3
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Expression Region
1-363aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAPAGRPGAKKGILERLESGEVVIGDG SFLITLEKRGYVKAGLWTPEAVIEHPDAVRQLHMEFLRAGSNVMQTFTFS ASEDNMESKWEDVNAAACDLAREVAGKGDALVAGGICQTSIYKYQKDEAR IKKLFRQQLEVFAWKNVDFLIAEYFEHVEEAVWAVEVLKESDRPVAVTMC IGPEGDMHDITPGECAVRLVKAGASIVGVNCRFGPDTSLKTMELMKEGLE WAGLKAHLMVQPLGFHAPDCGKEGFVDLPEYPFGLESRVATRWDIQKYAR EAYNLGVRYIGGCCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLD MHTKPWIRARARREYWENLLPASGRPFCPSLSKPDF
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Molecular Weight
43 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
BHMT2 (Betaine-Homocysteine Methyltransferase 2) is a recently identified enzyme that plays a crucial role in the methionine cycle by catalyzing the transfer of a methyl group from betaine to homocysteine, forming dimethylglycine and thereby regulating homocysteine levels in the body. Elevated homocysteine has been implicated in various health issues, including cardiovascular diseases and neurodegenerative disorders. Research into BHMT2 is gaining momentum due to its potential implications for health and disease management. The enzyme's structure, substrate specificity, and kinetic properties are of particular interest for understanding its therapeutic potential. With the advent of recombinant DNA technology, producing BHMT2 as a recombinant protein allows for in-depth biochemical and functional analyses. Such studies can uncover its role in metabolic pathways and its interaction with co-factors, ultimately leading to insights into how modulation of BHMT2 activity could serve as a strategy for addressing diseases related to homocysteine metabolism. This exploration not only contributes to our fundamental understanding of human biochemistry but also opens avenues for developing novel therapeutic approaches targeting dysregulated methylation processes linked to various pathological conditions.
