Analytical Data
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Gene name
SULT1C4
- Application
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Alternative Names
SULT1C4；SULT1C2；Sulfotransferase 1C4
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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
O75897
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Expression Region
1-302aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MALHDMEDFT FDGTKRLSVN YVKGILQPTD TCDIWDKIWN FQAKPDDLLI STYPKAGTTW TQEIVELIQN EGDVEKSKRA PTHQRFPFLE MKIPSLGSGL EQAHAMPSPR ILKTHLPFHL LPPSLLEKNC KIIYVARNPK DNMVSYYHFQ RMNKALPAPG TWEEYFETFL AGKVCWGSWH EHVKGWWEAK DKHRILYLFY EDMKKNPKHE IQKLAEFIGK KLDDKVLDKI VHYTSFDVMK QNPMANYSSI PAEIMDHSIS PFMRKGAVGD WKKHFTVAQN ERFDEDYKKK MTDTRLTFHF QF
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Molecular Weight
38 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
SULT1C4, a member of the sulfotransferase family, plays a significant role in the metabolism of various endogenous compounds and xenobiotics by catalyzing the sulfation process, which is crucial for their biological inactivation and elimination. The enzyme's function has gained attention due to its involvement in the detoxification of drugs and potential implications in pharmacogenomics. Research has shown that SULT1C4 may be involved in steroid hormone metabolism, thereby influencing physiological processes and potentially affecting susceptibility to diseases such as cancer and cardiovascular disorders. Despite its importance, the biochemical properties, substrate specificity, and regulation of SULT1C4 remain poorly understood, primarily due to difficulties in obtaining sufficient quantities of the enzyme for study. Recent advances in recombinant protein technology have facilitated the production of SULT1C4 in heterologous systems, allowing for detailed structural and functional analyses. Investigations into the enzyme’s kinetics and interaction with various substrates may uncover its physiological roles and contribute to the understanding of individual variations in drug response. Additionally, elucidating the molecular mechanisms governing SULT1C4’s activity could provide insights into disease mechanisms and lead to the development of targeted therapies. Overall, the exploration of SULT1C4 as a recombinant protein holds promise for advancing our understanding of its biological significance and potential applications in clinical settings.
