Analytical Data
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Gene name
AHCY
- Application
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Alternative Names
SAHH; AdoHcyase; S-Adenosylhomocysteine Hydrolase; S-adenosyl-L-homocysteine hydrolase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P23526
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Expression Region
Ser2~Tyr432
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Molecular Weight
48kDa
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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
AHCY (S-Adenosylhomocysteine hydrolase) is an important enzyme involved in the methionine cycle and transmethylation processes, playing a crucial role in regulating levels of S-adenosylhomocysteine (SAH) and S-adenosylmethionine (SAM). Its dysfunction is linked to various pathological conditions, including cardiovascular diseases and certain cancers, making it a notable target for therapeutic interventions. Research in AHCY has gained momentum due to its potential implications in metabolic disorders and the emerging interest in epigenetic regulation through methylation processes in diseases. The characterization of recombinant AHCY proteins is pivotal for understanding enzyme mechanisms, substrate specificity, and potential inhibitors, which can pave the way for drug development. Advances in recombinant DNA technology have facilitated the production of AHCY proteins, enabling detailed biochemical and structural studies. Investigating AHCY through recombinant protein analysis also opens doors for novel therapeutic strategies by modulating its activity, thereby influencing cellular methylation status and offering prospects for treating various diseases associated with aberrant methylation patterns. Hence, the study of recombinant AHCY proteins is integral to both fundamental biochemical research and the development of new biomedical applications.
