Analytical Data
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Gene name
HCy
- Application
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Alternative Names
HCy；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
Q12525
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Expression Region
1-324aa
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AA Sequence
MKRIPIKELIVEHPGKVLILDGGQGTELENRGININSPVWSAAPFTSESFWEPSSQERKVVEEMYRDFMIAGANILMTITYQANFQSISENTSIKTLAAYKRFLDKIVSFTREFIGEERYLIGSIGPWAAHVSCEYTGDYGPHPENIDYYGFFKPQLENFNQNRDIDLIGFETIPNFHELKAILSWDEDIISKPFYIGLSVDDNSLLRDGTTLEEISVHIKGLGNKINKNLLLMGVNCVSFNQSALILKMLHEHLPGMPLLVYPNSGEIYNPKEKTWHRPTNKLDDWETTVKKFVDNGARIIGGCCRTSPKDIAEIASAVDKYS
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Molecular Weight
40.7 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
Homocysteine (HCy) is a sulfur-containing amino acid that plays a significant role in various biological processes, including protein synthesis and methylation reactions. Elevated levels of homocysteine in the bloodstream, known as hyperhomocysteinemia, have been associated with a range of health issues, particularly cardiovascular diseases, neurodegenerative disorders, and complications during pregnancy. The metabolism of homocysteine involves several key enzymes and cofactors, including vitamins B6, B12, and folate, which work together to convert homocysteine into cysteine or methionine. Research into HCy recombinant proteins seeks to better understand HCy metabolism and its implications for human health. Recombinant technology allows for the production of homocysteine-related proteins, enabling scientists to study their structure and function in detail, as well as to explore potential therapeutic applications for conditions linked to abnormal HCy levels. The exploration of HCy's role in epigenetic regulation, inflammation, and cellular signaling further underscores the importance of understanding its biochemical pathways. By creating recombinant forms of enzymes involved in HCy metabolism, studies can elucidate their mechanisms of action and their influence on health, paving the way for new diagnostic and treatment strategies for diseases associated with HCy dysregulation.
