Analytical Data
-
Gene name
NELFB
- Application
-
Alternative Names
Cofactor of BR;CA1
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WX92
-
Expression Region
8-199aa
-
Molecular Weight
48.9 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 (Negative Elongation Factor B) is a crucial protein involved in the regulation of gene expression at the transcriptional level. It plays a significant role in RNA polymerase II (Pol II) elongation by interacting with other factors and modulating transcriptional pauses. The expression and activity of NELFB have been linked to various cellular processes, including cellular growth, differentiation, and response to stress. The dysfunction of NELFB has been implicated in several diseases, including cancers and neurodegenerative disorders, making it a potential target for therapeutic interventions. Studying NELFB and its interactions with other transcriptional machinery components can provide valuable insights into the fundamental mechanisms of gene transcription and regulation. Recent advancements in recombinant protein technology enable the production of NELFB in controlled laboratory settings, facilitating detailed structural and functional studies. This research is essential for understanding the molecular basis of its actions in normal cellular physiology and pathological conditions, and it may lead to the development of novel strategies for modulating NELFB activity in disease contexts.
