Analytical Data
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Gene name
NUBPL
- Application
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Alternative Names
C14orf127; FLJ12660; huInd1; IND1 homolog; Iron-sulfur protein NUBPL; Nubpl; NUBPL_HUMAN; nucleotide binding protein like; Nucleotide-binding protein-like
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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
Q8TB37
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Expression Region
39-319 aa
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AA Sequence
GA GSETLKQRRT QIMSRGLPKQ KPIEGVKQVI VVASGKGGVG KSTTAVNLAL ALAANDSSKA IGLLDVDVYG PSVPKMMNLK GNPELSQSNL MRPLLNYGIA CMSMGFLVEE SEPVVWRGLM VMSAIEKLLR QVDWGQLDYL VVDMPPGTGD VQLSVSQNIP ITGAVIVSTP QDIALMDAHK GAEMFRRVHV PVLGLVQNMS VFQCPKCKHK THIFGADGAR KLAQTLGLEV LGDIPLHLNI REASDTGQPI VFSQPESDEA KAYLRIAVEV VRRLPSPSE
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Molecular Weight
34.0 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
NUBPL (Nuclear-Binding Protein-Like), a crucial protein involved in various cellular processes, has garnered significant interest in recent years due to its role in mitochondrial function and cellular metabolism. Initial studies have linked NUBPL to the assembly and activity of iron-sulfur (Fe-S) clusters, which are essential components for many mitochondrial enzymes and critical for maintaining cellular energy homeostasis. Dysregulation of NUBPL has been implicated in several pathological conditions, including neurodegenerative diseases and metabolic disorders, making its study vital for understanding these complex diseases. Researchers have also noted its potential involvement in the response to oxidative stress, further highlighting its importance in cellular defense mechanisms. The recombinant expression and purification of NUBPL in various systems have enabled in-depth biochemical characterization, allowing researchers to investigate its structure-function relationships and interactions with other mitochondrial proteins. By elucidating the mechanistic pathways involving NUBPL, this research aims to uncover potential therapeutic targets for treating diseases linked to mitochondrial dysfunction, thereby contributing to the development of novel strategies for disease intervention. As the understanding of NUBPL’s role in cellular biology continues to grow, it promises to be a key player in the broader context of mitochondrial research and its implications for human health.
