NGFR Human

Nerve Growth Factor Receptor Human Recombinant
Cat. No.
BT7112
Source
Sf9, Baculovirus cells.
Synonyms
Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

NGFR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 230 amino acids (29-250 a.a.) and having a molecular mass of 24.6kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).
NGFR is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Tumor necrosis factor receptor superfamily member 16 (NGFR) is part of the tumor necrosis factor receptor superfamily. It is widely expressed in tissues including the brain, liver, lung, and muscle. NGFR plays a role in regulating the movement of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin. It may achieve this by regulating RAB31 activity, thereby contributing to the regulation of insulin-dependent glucose uptake. NGFRs are low-affinity receptors that can bind to NGF, BDNF, NT-3, and NT-4. NGFR is involved in both cell survival and cell death of neural cells.
Description
NGFR, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It consists of 230 amino acids (29-250 a.a.) and has a molecular mass of 24.6kDa. On SDS-PAGE under reducing conditions, it migrates at 40-57kDa. An 8 amino acid His tag is present at the C-Terminus of the expressed NGFR. Purification is carried out using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The NGFR protein solution has a concentration of 1mg/ml. It is prepared in a Phosphate Buffered Saline solution at pH 7.4 with 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For longer storage periods, it should be stored frozen at -20°C. For long-term storage, it is advisable to add a carrier protein (either HSA or BSA) at a concentration of 0.1%. Repeated freezing and thawing of the product should be avoided.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Synonyms
Tumor necrosis factor receptor superfamily member 16, Gp80-LNGFR, Low affinity neurotrophin receptor p75NTR, Low-affinity nerve growth factor receptor, NGF receptor, p75 ICD, CD271.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
KEACPTGLYT HSGECCKACN LGEGVAQPCG ANQTVCEPCL DSVTFSDVVS ATEPCKPCTE CVGLQSMSAP CVEADDAVCR CAYGYYQDET TGRCEACRVC EAGSGLVFSC QDKQNTVCEE CPDGTYSDEA NHVDPCLPCT VCEDTERQLR ECTRWADAEC EEIPGRWITR STPPEGSDST APSTQEPEAP PEQDLIASTV AGVVTTVMGS SQPVVTRGTT DNLEHHHHHH.

Product Science Overview

Introduction

The Nerve Growth Factor (NGF) receptor, also known as TrkA (tropomyosin receptor kinase A), is a critical component in the neurotrophin family. This receptor plays a pivotal role in the development, maintenance, and function of the nervous system. The recombinant form of the human NGF receptor has been extensively studied for its therapeutic potential in various neurological disorders.

Discovery and Structure

The discovery of NGF dates back to the 1950s, with the pioneering work of Rita Levi-Montalcini and Stanley Cohen, who were awarded the Nobel Prize for their groundbreaking research. NGF was the first neurotrophin to be identified, and it paved the way for the discovery of other neurotrophins such as brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4).

The NGF receptor, TrkA, is a transmembrane protein that belongs to the receptor tyrosine kinase family. It consists of an extracellular ligand-binding domain, a single transmembrane helix, and an intracellular tyrosine kinase domain. The binding of NGF to TrkA induces receptor dimerization and autophosphorylation, leading to the activation of downstream signaling pathways that promote neuronal survival, differentiation, and growth .

Function and Mechanism

The primary function of the NGF receptor is to mediate the effects of NGF on neurons. NGF binds to TrkA with high affinity, triggering a cascade of intracellular events that support neuronal survival and growth. This interaction is crucial during the development of the nervous system, as it ensures the proper formation and maintenance of neural circuits.

In addition to its role in the peripheral nervous system, NGF and its receptor are also involved in the central nervous system. They play a significant role in the maintenance of cholinergic neurons in the basal forebrain, which are essential for cognitive functions such as learning and memory .

Therapeutic Applications

The recombinant form of the human NGF receptor has shown promise in various therapeutic applications. One of the most notable advancements is the development of cenegermin-bkbj, a recombinant human NGF approved by the United States Food and Drug Administration (FDA) for the treatment of neurotrophic keratitis, a rare degenerative disease of the cornea .

Research is ongoing to explore the potential of recombinant NGF and its receptor in treating other neurological conditions, such as Alzheimer’s disease, peripheral neuropathies, and traumatic brain injuries. The ability of NGF to promote neuronal survival and regeneration makes it a promising candidate for neuroprotective therapies .

Challenges and Future Directions

Despite the therapeutic potential of recombinant NGF and its receptor, several challenges remain. One of the primary obstacles is the difficulty in delivering NGF to the target tissues in a controlled and sustained manner. Additionally, the potential side effects and the complexity of the production process pose significant hurdles.

Future research is focused on developing innovative delivery strategies, such as gene therapy and nanotechnology-based approaches, to overcome these challenges. Advances in our understanding of the molecular mechanisms underlying NGF signaling will also contribute to the development of more effective and targeted therapies .

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