Analytical Data
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Gene name
NGFR
- Application
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Alternative Names
BEX3; Bex; HGR74; NADE; Brain Expressed,X-Linked 3; Ovarian granulosa cell 13.0 kDa protein HGR74; p75NTR-associated cell death executor
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by reducing SDS-PAGE.
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Uniprot
Q00994
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Expression Region
Met1~Pro111
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Molecular Weight
43kDa
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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
The nerve growth factor receptor (NGFR), also known as p75 neurotrophin receptor (p75NTR), plays a crucial role in the development and maintenance of the nervous system by mediating the effects of neurotrophins, such as nerve growth factor (NGF). Research into NGFR has gained prominence due to its involvement in various neurodegenerative diseases, including Alzheimer's disease and Amyotrophic Lateral Sclerosis (ALS). The receptor is unique as it can trigger both pro-survival and pro-apoptotic signaling pathways depending on the cellular context and the presence of other neurotrophic factors. Understanding the structure and functioning of NGFR, specifically through the development and characterization of recombinant NGFR proteins, has become essential for elucidating its dual roles in neuronal health and disease. These recombinant proteins can be utilized in vitro to investigate ligand-binding interactions and downstream signaling pathways, thus providing insights into their therapeutic potential. Additionally, the study of NGFR can enhance our understanding of cellular responses to stress and injury, making it a target of interest for drug discovery aimed at modulating its activity in neurodegenerative conditions. By developing reliable expression systems and purification methods, researchers aim to produce high-quality NGFR proteins that can be employed in various experimental settings, ultimately contributing to the advancement of neurological research and potential therapeutic interventions.
