Analytical Data
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Gene name
RSAD1
- Application
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Alternative Names
RSAD1; Radical S-adenosyl methionine domain-containing protein 1; mitochondrial; Putative heme chaperone
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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
Q9HA92
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Expression Region
18-442 aa
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AA Sequence
AQR RRRVENAGGS PSPEPAGRRA ALYVHWPYCE KRCSYCNFNK YIPRRLEEAA MQKCLVTEAQ TLLRLSGVQR VESVFFGGGT PSLASPHTVA AVLEAVAQAA HLPADLEVTL EANPTSAPGS RLAEFGAAGV NRLSIGLQSL DDTELRLLGR THSACDALRT LAEARRLFPG RVSVDLMLGL PAQQVGPWLG QLQELLHHCD DHLSLYQLSL ERGTALFAQV QRGALPAPDP ELAAEMYQRG RAVLREAGFH QYEVSNFARN GALSTHNWTY WQCGQYLGVG PGAHGRFMPQ GAGGHTREAR IQTLEPDNWM KEVMLFGHGT RKRVPLGRLE LLEEVLALGL RTDVGITHQH WQQFEPQLTL WDVFGANKEV QELLERGLLQ LDHRGLRCSW EGLAVLDSLL LTLLPQLQEA WQQRTPSPVP GG
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Molecular Weight
48.7 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
RSAD1 (Radical S-adenosyl methionine domain-containing protein 1) is a crucial protein involved in the innate immune response, especially in the context of viral infections. It was initially identified as an interferon-stimulated gene, suggesting that its expression is upregulated in response to viral pathogens. Research has shown that RSAD1 plays a significant role in antiviral defense by participating in the formation of protective structures called "vacuoles," which can sequester viral components and inhibit virus replication. Furthermore, RSAD1 has been implicated in various cellular processes, including apoptosis and autophagy, highlighting its multifaceted role in cellular homeostasis and immune regulation. Given its potential as a therapeutic target, studies have been focusing on the functional properties of RSAD1, particularly its ability to interact with cellular machinery to modulate immune responses and its implications in diseases linked to viral infections. Understanding the molecular mechanisms underlying RSAD1 function and its regulatory pathways can provide insights into novel antiviral strategies and enhance our knowledge of immune system dynamics. Therefore, the study of RSAD1 and its recombinant protein form has gained significant attention, as it could lead to new therapeutic interventions against viral diseases and further our understanding of immune modulation.
