Analytical Data
-
Gene name
NENF
- Application
-
Alternative Names
CIR2; SCIRP10; NDNF; SPUF; Neudesin; Cell immortalization-related protein 2; Neuron-derived neurotrophic factor; Secreted protein of unknown function
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UMX5
-
Expression Region
Gly32~Phe172
-
Molecular Weight
19kDa
-
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
NENF, or Neuronal Enriched Neurofilament Protein, is a significant component of the neuronal cytoskeleton, playing a crucial role in maintaining neuronal structure, stability, and function. Research into NENF recombinant proteins has gained momentum due to their potential applications in understanding neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS) and Alzheimer's disease, where neurofilament abnormalities are often observed. By producing NENF in a recombinant form, scientists aim to investigate its biochemical properties, interactions with other cytoskeletal components, and its role in neuronal health and pathology. This research can enhance our understanding of the mechanisms underlying neuronal degeneration and may facilitate the development of therapeutic strategies targeting neurofilament aggregation or misfolding. Furthermore, recombinant NENF proteins can be utilized as valuable tools in the study of neuronal function and the dynamics of neurofilament transport, offering insights into cellular processes essential for neuronal survival. The advancement of techniques in protein engineering and expression systems has significantly improved the ability to produce high-quality NENF recombinant proteins, fostering further exploration into their functional implications in both healthy and diseased states of the nervous system. Overall, the study of NENF recombinant proteins holds promise for unveiling novel pathways in neurobiology and contributes to a deeper understanding of the complex interactions that sustain neuronal integrity and function.
