b NGF Human, HEK

beta Nerve Growth Factor Human Recombinant, HEK
Cat. No.
BT6772
Source

HEK293 cells.

Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity

Greater than 97% as obsereved by SDS-PAGE.

Usage
THE BioTeks 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

BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

Product Specs

Introduction
NGF-beta, also known as nerve growth factor beta, is a protein involved in the growth and differentiation of nerve cells, particularly sympathetic and certain sensory neurons. It plays a role in the development and maintenance of the nervous system. Mutations in the gene encoding NGF-beta can lead to hereditary sensory and autonomic neuropathy type 5 (HSAN5), a disorder characterized by sensory impairments and autonomic dysfunction. Additionally, abnormal expression of this gene is linked to allergic rhinitis.
Description
Recombinant human BNGF, produced in HEK293 cells, is a homodimeric protein consisting of two identical polypeptide chains linked by a disulfide bond. Each chain contains 118 amino acids (Ser122-Arg239) and has a molecular weight of 26.5 kDa. The protein is glycosylated, meaning it has sugar molecules attached.
Physical Appearance
White powder, sterile-filtered and lyophilized.
Formulation
The b-NGF was lyophilized in a solution containing 20mM PB (phosphate buffer), 0.25M NaCl (sodium chloride) at a pH of 7.5. The initial concentration before lyophilization was 1mg/ml.
Solubility
To reconstitute the lyophilized b-NGF, it is recommended to dissolve it in sterile, pyrogen-free distilled water at a concentration of 0.25mg/ml.
Stability
Lyophilized b-NGF is stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store it desiccated at a temperature below -18°C. After reconstitution, the b-NGF solution can be stored at 4°C for 2-7 days. For longer storage periods, it is advisable to store it below -18°C. To enhance stability during long-term storage, consider adding a carrier protein such as HSA (human serum albumin) or BSA (bovine serum albumin) at a concentration of 0.1%. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the b-NGF is greater than 97% as determined by SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis).
Biological Activity
The biological activity of b-NGF was assessed by its ability to stimulate the proliferation of human TF-1 cells, which are erythroleukemic indicator cells. The ED50, which represents the concentration of b-NGF required to achieve 50% of the maximum proliferation response, is less than 0.04-0.4 ng/ml.
Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Source

HEK293 cells.

Product Science Overview

Introduction

Beta Nerve Growth Factor (β-NGF) is a crucial neurotrophic factor that plays a significant role in the development, maintenance, and survival of neurons. It belongs to the nerve growth factor protein superfamily and is involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons .

Discovery and Historical Context

The discovery of NGF dates back to the pioneering work of Nobel Prize winner Rita Levi-Montalcini, who identified its role in neuronal growth and survival. This groundbreaking research laid the foundation for understanding the complex mechanisms of neurotrophic factors and their therapeutic potential .

Structure and Production

Human recombinant β-NGF is produced using HEK293 cells, a type of human embryonic kidney cell line. The recombinant form is a noncovalently disulfide-linked homodimer, glycosylated polypeptide chain containing 118 amino acids with a molecular mass of 26.5 kDa . This production method ensures high purity and biological activity, making it suitable for research and therapeutic applications .

Biological Functions

β-NGF is a key mediator in neuronal and non-neuronal development, differentiation, and survival. It binds to the tyrosine kinase A receptor with high affinity and to the p75 neurotrophin receptor with low affinity . This binding triggers signaling pathways that promote neuronal growth, survival, and regeneration .

Clinical Applications

The clinical application of β-NGF has been explored in various therapeutic areas. One notable example is the FDA-approved drug cenegermin-bkbj, a recombinant human NGF used for the treatment of neurotrophic keratitis . This approval marks a significant milestone in translating NGF research into practical medical treatments.

Challenges and Future Directions

Despite its potential, the clinical application of β-NGF has faced challenges, including determining appropriate dosing, administration strategies, and production complexities . However, ongoing research and advancements in biotechnology continue to address these challenges, paving the way for broader therapeutic applications.

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