Analytical Data
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Gene name
AHCY
- Application
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Alternative Names
AHCY；DCAL；IRBIT；XPVKONA；S-adenosylhomocysteine hydrolase-like Protein 1
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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
P23526
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Expression Region
1 -432aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSDKLPYKVADIGLAAWGRKALDIAENEMP GLMRMRERYSASKPLKGARIAGCLHMTVETAVLIETLVTLGAEVQWSSCN IFSTQDHAAAAIAKAGIPVYAWKGETDEEYLWCIEQTLYFKDGPLNMILD DGGDLTNLIHTKYPQLLPGIRGISEETTTGVHNLYKMMANGILKVPAINV NDSVTKSKFDNLYGCRESLIDGIKRATDVMIAGKVAVVAGYGDVGKGCAQ ALRGFGARVIITEIDPINALQAAMEGYEVTTMDEACQEGNIFVTTTGCID IILGRHFEQMKDDAIVCNIGHFDVEIDVKWLNENAVEKVNIKPQVDRYRL KNGRRIILLAEGRLVNLGCAMGHPSFVMSNSFTNQVMAQIELWTHPDKYP VGVHFLPKKLDEAVAEAHLGKLNVKLTKLTEKQAQYLGMSCDGPFKPDHY RY
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Molecular Weight
50 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
AHCY (Adenosylhomocysteinase) is an essential enzyme that catalyzes the hydrolysis of adenosylhomocysteine to adenosine and homocysteine, playing a critical role in the methionine cycle and regulating the levels of S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH). Dysregulation of AHCY has been implicated in various pathological conditions including cardiovascular diseases, neurological disorders, and certain cancers. Research on recombinant AHCY protein has gained momentum in recent years, as it provides a valuable tool for elucidating the structure-function relationship of the enzyme, exploring its metabolic pathways, and investigating its potential as a therapeutic target. The production of recombinant AHCY not only allows for detailed biochemical characterization but also facilitates the development of inhibitors that may have therapeutic applications in treating diseases associated with altered homocysteine metabolism. Furthermore, understanding the dynamics of AHCY activity and its regulation can lead to insights into cellular methylation processes, which are pivotal for gene expression and epigenetic modifications. As such, AHCY remains a significant focus of biochemical research, with ongoing studies aimed at optimizing its expression and purification methods, improving assay techniques, and exploring its interactions with other biomolecules within the context of metabolic and signaling pathways. Through these investigations, researchers hope to uncover new avenues for clinical interventions and advance knowledge in the fields of molecular biology and pharmacology.
