Analytical Data
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Gene name
NELFB
- Application
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Alternative Names
NELFB；COBRA1；KIAA1182；Negative elongation factor B
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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
Q8WX92
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Expression Region
8-199aa
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AA Sequence
LGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGE
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Molecular Weight
48.9 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
NELFB, or Negative Elongation Factor B, is a key player in the regulation of transcription elongation in eukaryotic cells. It is part of a multi-subunit complex that interacts with RNA polymerase II, influencing the transition from the initiation phase of transcription to the elongation phase. The dysfunction of NELFB has been implicated in various diseases, including cancer and viral infections, where its role in modulating transcriptional processes may be exploited by pathological states. Research on NELFB recombinant proteins is vital for understanding its structural biology, functional mechanisms, and interactions with other transcription factors. By producing recombinant NELFB proteins, scientists can investigate their biochemical properties, perform binding affinity studies, and elucidate the molecular mechanisms that regulate gene expression. This understanding may offer insights into novel therapeutic targets for treating diseases associated with transcriptional dysregulation. The study of NELFB not only advances our comprehension of fundamental cellular processes but also contributes to the broader field of epigenetics and gene regulation.
