Analytical Data
-
Gene name
NGF
- Application
-
Alternative Names
Ngf; Ngfb; Beta-nerve growth factor; Beta-NGF
-
Species
Rat
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P25427
-
Expression Region
124-241aa
-
Protein Length
Partial
-
Molecular Weight
17.2 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
Nerve Growth Factor (NGF) is a pivotal neurotrophic factor primarily involved in the growth, maintenance, and survival of neurons. Its discovery in the 1950s marked a significant advancement in neurobiology, leading to an enhanced understanding of neuronal development and the mechanisms underlying neurodegenerative diseases. NGF is not only crucial for the development of sensory and sympathetic neurons but also plays a role in modulating pain perception and inflammatory responses. The recombinant production of NGF has enabled researchers to explore its therapeutic potential in various neurological conditions, such as Alzheimer's disease, neuropathic pain, and spinal cord injuries. Advances in molecular biology techniques have facilitated the synthesis of NGF in engineered systems, ensuring a reliable supply for both basic research and clinical applications. Moreover, studies on NGF’s receptor interactions and signaling pathways have unveiled its complex role in neuroprotection and neuroinflammation. Current research focuses on optimizing NGF formulations to enhance stability and efficacy, aiming to translate these findings into effective therapies for neurodegenerative disorders. Consequently, recombinant NGF protein serves as a valuable tool in both fundamental research and therapeutic interventions, representing a promising avenue for improving neuronal health and addressing the challenges of neurodegenerative diseases.
