ProNGF Human

Pro-Nerve Growth Factor Human Recombinant
Cat. No.
BT7161
Source
Escherichia Coli.
Synonyms
Human Pro-NGF, ProNGF, NGFB.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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

Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.
ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

Product Specs

Description
Recombinant Human Pro-NGF, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 224 amino acids. It exhibits a molecular weight of 25 kDa. The purification process involves proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
ProNGF was lyophilized from a 0.2 µM filtered solution containing 20mM Tris-HCL (pH 8.0), 0.5M NaCl, 5% Trehalose, 5% Mannitol, 0.01% Tween-80, and 1mM EDTA.
Solubility
Reconstitute the lyophilized ProNGF in distilled water to a minimum concentration of 100 µg/ml. This solution can be further diluted into other aqueous solutions as needed.
Stability
Lyophilized ProNGF remains stable at room temperature for up to 3 weeks. However, for long-term storage, it should be stored desiccated below -18°C. After reconstitution, ProNGF should be stored at 4°C for 2-7 days. For extended storage, it should be kept below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms
Human Pro-NGF, ProNGF, NGFB.
Source
Escherichia Coli.
Amino Acid Sequence

MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA.

Product Science Overview

Introduction

Pro-Nerve Growth Factor (Pro-NGF) is a precursor protein to Nerve Growth Factor (NGF), a crucial molecule involved in the development, maintenance, and survival of neurons. NGF was the first neurotrophin discovered and has been extensively studied for its role in neuroregulation and disease pathogenesis .

Discovery and Historical Context

The discovery of NGF dates back to the pioneering work of Nobel Prize winner Rita Levi-Montalcini. Her groundbreaking research laid the foundation for understanding the physiological roles of neurotrophins, including NGF . Over the years, advancements in biotechnology have enabled the production of recombinant forms of these proteins, including Pro-NGF.

Characteristics and Production

Pro-NGF human recombinant is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 224 amino acids with a molecular mass of 25 kDa . The recombinant protein is purified using proprietary chromatographic techniques to ensure high purity and stability. It is typically lyophilized (freeze-dried) for storage and reconstituted in distilled water for use in research and therapeutic applications .

Biological Functions

Pro-NGF plays a significant role in neuronal development, synaptic plasticity, and cell survival. It is involved in various signaling pathways that regulate neuronal health and function. The precursor form, Pro-NGF, must be cleaved to generate mature NGF, which then exerts its biological effects by binding to specific receptors on the surface of neurons .

Clinical Applications and Research

Recent advances in the production and scientific understanding of recombinant NGF have led to its clinical development. In 2018, the United States Food and Drug Administration (FDA) approved cenegermin-bkbj, a recombinant human NGF, for the treatment of neurotrophic keratitis, a degenerative eye disease . This approval marked a significant milestone in the therapeutic application of NGF and opened new avenues for research into its potential uses in other neurological disorders and neurodegenerative diseases .

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