Analytical Data
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Gene name
SEPHS2
- Application
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Alternative Names
SEPHS2；SPS2；Selenide. water dikinase 2
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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
Q99611
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Expression Region
2-448aa
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AA Sequence
AEASATGACGEAMAAAEGSSGPAGLTLGRSFSNYRPFEPQALGLSPSWRLTGFSGMKGSGCKVPQEALLKLLAGLTRPDVRPPLGRGLVGGQEEASQEAGLPAGAGPSPTFPALGIGMDSCVIPLRHGGLSLVQTTDFFYPLVEDPYMMGRIACANVLSDLYAMGITECDNMLMLLSVSQSMSEEEREKVTPLMVKGFRDAAEEGGTAVTGGQTVVNPWIIIGGVATVVCQPNEFIMPDSAVVGDVLVLTKPLGTQVAVNAHQWLDNPERWNKVKMVVSREEVELAYQEAMFNMATLNRTAAGLMHTFNAHAATDITGFGILGHSQNLAKQQRNEVSFVIHNLPIIAKMAAVSKASGRFGLLQGTSAETSGGLLICLPREQAARFCSEIKSSKYGEGHQAWIVGIVEKGNRTARIIDKPRVIEVLPRGATAAVLAPDSSNASSEPSS
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Molecular Weight
54.6 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
SEPHS2 (Serine Hydroxymethyltransferase 2) is a key enzyme involved in the one-carbon metabolic pathway, which plays a crucial role in cellular processes such as nucleotide synthesis and amino acid metabolism. The enzyme catalyzes the conversion of serine to glycine, alongside the transfer of a hydroxymethyl group to tetrahydrofolate, thereby participating in the generation of crucial one-carbon units necessary for the biosynthesis of purines and thymidine. Research on SEPHS2 has gained attention due to its potential implications in various biological contexts, including cell proliferation, differentiation, and the pathogenesis of diseases such as cancer. Abnormal expression or activity of SEPHS2 has been linked to altered metabolic states in several cancers, underscoring the importance of understanding its structure and function. Furthermore, the exploration of SEPHS2 as a potential therapeutic target has been spurred by its pivotal role in cancer metabolism. In this context, the expression and characterization of recombinant SEPHS2 proteins are essential for elucidating its enzymatic mechanisms, substrate specificity, and interactions with other proteins and metabolites. By utilizing recombinant DNA technology to produce SEPHS2 in heterologous systems, researchers can generate sufficient quantities of the enzyme for detailed biochemical studies. These efforts will contribute significantly to our understanding of the functional dynamics of SEPHS2, helping to unravel its contributions to metabolic regulation and disease processes, ultimately paving the way for novel therapeutic strategies targeting metabolic pathways associated with this enzyme.
