Analytical Data
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Gene name
AARSD1
- Application
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Alternative Names
Alanyl-tRNA editing protein Aarsd1; Alanyl-tRNA synthetase domain-containing protein 1; AARSD1
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q9BTE6-2
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Expression Region
T176-E525
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AA Sequence
TINDISVLRVTRRGEQADHFTQTPLDPGSQVLVRVDWERRFDHMQQHSGQHLITAVADHLFKLKTTSWELGRFRSAIELDTPSMTAEQVAAIEQSVNEKIRDRLPVNVRELSLDDPEVEQVSGRGLPDDHAGPIRVVNIEGVDSNMCCGTHVSNLSDLQVIKILGTEKGKKNRTNLIFLSGNRVLKWMERSHGTEKALTALLKCGAEDHVEAVKKLQNSTKILQKNNLNLLRDLAVHIAHSLRNSPDWGGVVILHRKEGDSEFMNIIANEIGSEETLLFLTVGDEKGGGLFLLAGPPASVETLGPRVAEVLEGKGAGKKGRFQGKATKMSRRMEAQALLQDYISTQSAKE
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Protein Length
Partial
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Molecular Weight
40 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
AARSD1, or Arylsulfatase D1, is a recently identified member of the arylsulfatase family, which plays a crucial role in the hydrolysis of sulfate esters in various biological processes. Research on AARSD1 has gained momentum due to its potential implications in human health and disease, particularly in the context of metabolic disorders and neurological conditions. The enzyme's activity is linked to the degradation of sulfated metabolites, which are vital for cellular signaling, hormone regulation, and the maintenance of extracellular matrix components. Studies have shown that mutations or dysregulation of AARSD1 can contribute to pathological states, emphasizing the need for detailed investigation into its structure and function. Recombinant expression of AARSD1 allows for the production of the protein in a controlled laboratory environment, facilitating the exploration of its enzymatic properties and substrate specificity. Understanding the mechanistic details of AARSD1 can aid in uncovering its biological significance, potential role as a biomarker, and suitability as a therapeutic target. The ongoing research aims to elucidate the function of this enzyme in various physiological and pathological contexts, providing insights that could lead to novel interventions for diseases associated with sulfate metabolism dysfunction.
