Analytical Data
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Gene name
NMRAL1
- Application
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Alternative Names
NMRAL1;HSCARG;NmrA-like family domain-containing Protein 1
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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
Q9HBL8
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Expression Region
1-299aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVDKKL VVVFGGTGAQ GGSVARTLLE DGTFKVRVVT RNPRKKAAKE LRLQGAEVVQ GDQDDQVIME LALNGAYATF IVTNYWESCS QEQEVKQGKL LADLARRLGL HYVVYSGLEN IKKLTAGRLA AAHFDGKGEV EEYFRDIGVP MTSVRLPCYF ENLLSHFLPQ KAPDGKSYLL SLPTGDVPMD GMSVSDLGPV VLSLLKMPEK YVGQNIGLST CRHTAEEYAA LLTKHTRKVV HDAKMTPEDY EKLGFPGARD LANMFRFYAL RPDRDIELTL RLNPKALTLD QWLEQHKGDF NLL
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Molecular Weight
36 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
NMRAL1, a member of the NMR family of proteins, has gained significant attention in recent years due to its potential roles in cellular processes and disease mechanisms. This protein is primarily implicated in the regulation of nitric oxide (NO) signaling and mitochondrial function, which are critical in various physiological and pathological contexts, including cancer, neurodegeneration, and cardiovascular diseases. The interest in NMRAL1 is further heightened by its involvement in the oxidative stress response and the modulation of gene expression through interactions with various transcription factors. Research has shown that NMRAL1 can influence cellular redox states, suggesting a vital role in maintaining homeostasis and cellular health. However, the molecular mechanisms underlying NMRAL1 functions remain poorly understood. Consequently, the development of recombinant NMRAL1 proteins for biochemical and biophysical studies has become essential to elucidate its structure-function relationships and to explore its potential as a therapeutic target. Recent advances in recombinant protein expression techniques have opened new avenues to investigate the detailed roles of NMRAL1 in various biological systems, enabling researchers to analyze its interactions, post-translational modifications, and effects on cellular metabolism. Understanding NMRAL1's role could provide insights into the development of novel strategies for treating diseases associated with impaired nitric oxide signaling and oxidative stress. Thus, the study of NMRAL1 recombinant proteins represents a promising frontier in both basic research and the quest for innovative therapeutic approaches.
