Analytical Data
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Gene name
SULT4A1
- Application
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Alternative Names
SULT4A1;SULTX3;Sulfotransferase 4A1
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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
Q9BR01
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Expression Region
1-284aa
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AA Sequence
MAESEAETPSTPGEFESKYFEFHGVRLPPFCRGKMEEIANFPVRPSDVWI VTYPKSGTSLLQEVVYLVSQGADPDEIGLMNIDEQLPVLEYPQPGLDIIK ELTSPRLIKSHLPYRFLPSDLHNGDSKVIYMARNPKDLVVSYYQFHRSLR TMSYRGTFQEFCRRFMNDKLGYGSWFEHVQEFWEHRMDSNVLFLKYEDMH RDLVTMVEQLARFLGVSCDKAQLEALTEHCHQLVDQCCSAEALPVGRGRV GLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL
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Molecular Weight
33 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
SULT4A1 (sulfotransferase family 4, member A1) is a member of the sulfotransferase enzyme family that plays a crucial role in the sulfation of various substrates, including neurotransmitters, steroids, and xenobiotics. It is unique among sulfotransferases due to its widespread distribution in the human brain, where it is implicated in modulating the activity of neurotransmitters and potentially influencing cognitive functions and neuropsychiatric disorders. Recent research has highlighted the importance of SULT4A1 in detoxification processes, as it participates in the metabolic inactivation of endogenous and exogenous compounds, thereby contributing to maintaining cellular homeostasis. Additionally, variations in the expression and activity of SULT4A1 have been correlated with susceptibility to neurological diseases, making it a target of interest for studying disease mechanisms and developing therapeutic interventions. Furthermore, the production of recombinant SULT4A1 protein enables detailed biochemical assays, structural studies, and the investigation of its role in sulfation pathways, paving the way for advances in pharmacology and toxicology. Understanding the function and regulation of SULT4A1 is crucial for elucidating its physiological significance and therapeutic potential.











