Analytical Data
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Gene name
ARSF
- Application
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Alternative Names
ARSF；Arylsulfatase F
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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
P54793
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Expression Region
23-590aa
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AA Sequence
HRVHDDKP NIVLIMVDDL GIGDLGCYGN DTMRTPHIDR LAREGVRLTQ HISAASLCSP SRSAFLTGRY PIRSGMVSSG NRRVIQNLAV PAGLPLNETT LAALLKKQGY STGLIGKWHQ GLNCDSRSDQ CHHPYNYGFD YYYGMPFTLV DSCWPDPSRN TELAFESQLW LCVQLVAIAI LTLTFGKLSG WVSVPWLLIF SMILFIFLLG YAWFSSHTSP LYWDCLLMRG HEITEQPMKA ERAGSIMVKE AISFLERHSK ETFLLFFSFL HVHTPLPTTD DFTGTSKHGL YGDNVEEMDS MVGKILDAID DFGLRNNTLV YFTSDHGGHL EARRGHAQLG GWNGIYKGGK GMGGWEGGIR VPGIVRWPGK VPAGRLIKEP TSLMDILPTV ASVSGGSLPQ DRVIDGRDLM PLLQGNVRHS EHEFLFHYCG SYLHAVRWIP KDDSGSVWKA HYVTPVFQPP ASGGCYVTSL CRCFGEQVTY HNPPLLFDLS RDPSESTPLT PATEPLHDFV IKKVANALKE HQETIVPVTY QLSELNQGRT WLKPCCGVFP FCLCDKEEEV SQPRGPNEKR
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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
ARSF, or Asparagine-Related Surface Protein, has garnered significant attention in recent years due to its potential implications in various biological processes and disease mechanisms. Initially identified in studies focused on cell signaling and protein interactions, ARSF is believed to play a crucial role in modulating neuronal function and sustaining cellular homeostasis. Its unique structure and surface properties suggest that it could be involved in the formation of protein complexes that influence cell communication and response to environmental stimuli. The recombinant expression of ARSF allows researchers to systematically investigate its biochemical characteristics, interactions, and functional role in different cellular contexts. Additionally, understanding the molecular mechanisms by which ARSF exerts its effects may reveal novel therapeutic targets for neurological disorders and other diseases associated with dysfunctional protein interactions. The advancement of recombinant technology has enabled the production of ARSF in sufficient quantities, facilitating the exploration of its structure-function relationships through various analytical techniques, including X-ray crystallography and nuclear magnetic resonance. Thus, the research on ARSF recombinant protein is not only pivotal for elucidating its biological significance but also for identifying potential applications in biotechnology and medicine.
