Analytical Data
-
Gene name
NGFIB
- Application
-
Alternative Names
GFRP1; HMR; N10; NAK-1; NGFIB; NP10; NUR77; TR3; DHR38; TIS1; Orphan nuclear receptor HMR; Testicular receptor 3; Nuclear receptor subfamily 4 group A member 1
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P22829
-
Expression Region
Gly264~Pro352
-
Molecular Weight
16kDa
-
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
The study of NGFIB (Nerve Growth Factor Inducible Protein B) recombinant proteins has garnered significant attention due to their potential roles in cellular signaling and neurobiology. NGFIB is a nuclear protein involved in modulating gene expression in response to nerve growth factor (NGF) stimulation, impacting neuronal survival, differentiation, and plasticity. Research has shown that NGFIB is crucial for various physiological processes, including neuronal development and response to stress. Given its involvement in neurogenic signaling pathways, understanding NGFIB’s structure and function can contribute to developing therapeutic strategies for neurodegenerative diseases and nerve injuries. The production of recombinant NGFIB proteins enables detailed studies of their biological activities, interactions with other cellular proteins, and their regulatory mechanisms in neural contexts. This research may also provide insights into how NGFIB modulation could be harnessed in regenerative medicine or neuroprotective therapies, paving the way for innovative treatment approaches that could enhance neuronal recovery and function in conditions such as Alzheimer's disease, Parkinson’s disease, and other neurological disorders. Overall, the investigation of NGFIB recombinant proteins represents a promising frontier in neuroscience and therapeutic development.











