NNT1 Human

Neurotrophin-1 Human Recombinant
Cat. No.
BT10969
Source
Escherichia Coli.
Synonyms
Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.
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

Neurotrophin-1 Human Recombinant (28-225) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 199 amino acids and having a molecular mass of 22kDa.
The NNT-1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neurotrophin-1 (NNT-1), also known as Cardiotrophin-like cytokine (CLC), is a protein belonging to the IL-6 cytokine family. This family utilizes the gp130 receptor subunit, a member of the type I cytokine receptor superfamily. NNT-1 exhibits several functions: promoting motor neuron survival, stimulating ACTH release from corticotrophs, and inducing IgE synthesis and B cell proliferation. Its expression is observed in various tissues during embryonic development, including muscle, lung epithelium, and mesenchyme. Functionally, NNT-1 binds to and activates the ILST/gp130 receptor complex.
Description
This product consists of the recombinant human Neurotrophin-1 (amino acids 28-225) expressed in E. coli. It is a single, non-glycosylated polypeptide chain composed of 199 amino acids, resulting in a molecular weight of 22 kDa. The purification process involves proprietary chromatographic techniques to ensure high purity.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The NNT-1 protein was lyophilized from a 0.2µm filtered solution containing Acetonitrile and TFA.
Solubility
To reconstitute the lyophilized NNT1, it is recommended to dissolve it in sterile 18M-cm H₂O to a concentration of at least 0.5 mg/ml. This solution can be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Neurotrophin-1 remains stable at room temperature for up to 3 weeks. However, for long-term storage, it is recommended to store the lyophilized powder desiccated at a temperature below -18°C. Once reconstituted, NNT1 should be stored at 4°C for a period of 2-7 days. For extended storage, it is advisable to add a carrier protein such as HSA or BSA (0.1%) and store the solution below -18°C. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 95.0% as determined by SDS-PAGE analysis.
Biological Activity
The biological activity of this product was determined by its ability to stimulate the proliferation of human TF-1 cells transfected with the human CNTF receptor. The ED₅₀, defined as the concentration of NNT-1 required to achieve half-maximal proliferation, is less than 15 ng/ml.
Synonyms
Cardiotrophin-Like Cytokine Factor 1, Novel Neurotrophin-1 , BSF3, CLC, CRLF1 Associated Cytokine-Like Factor 1, B-Cell Stimulating Factor 3, B-Cell-Stimulating Factor 3, BSF-3, NNT-1, NNT1, Neurotrophin-1/B-Cell Stimulating Factor-3, Cold-Induced Sweating Syndrome 2, B-Cell Stimulatory Factor 3, CISS2, NR6, CLCF1.
Source
Escherichia Coli.
Amino Acid Sequence
MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

Product Science Overview

Discovery and Early Research

The discovery of NGF marked a significant milestone in understanding the development and maintenance of the nervous system. Initially, NGF was characterized for its role in the sensory and autonomic nervous systems. Over time, its importance was recognized in the central nervous system, endocrine system, and immune system . NGF is essential for the development and phenotypic maintenance of neurons in the peripheral nervous system (PNS) and for the functional integrity of cholinergic neurons in the central nervous system (CNS) .

Physiological Role

NGF plays a crucial role in both the development and adulthood of neurons. It ensures the maintenance of phenotypic and functional characteristics of several populations of neurons as well as immune cells . The mature, active form of NGF is derived from the proteolytic cleavage of a precursor form known as ProNGF, which has both pro-apoptotic and neurotrophic properties .

Clinical Applications and Advances

Recent advances in the production and scientific knowledge of recombinant NGF have enabled its clinical development. In 2018, the United States Food and Drug Administration (FDA) approved cenegermin-bkbj, a recombinant human NGF, for the treatment of all stages of neurotrophic keratitis . This approval marked a significant step forward in the therapeutic application of NGF, highlighting its potential beyond the nervous system.

Future Prospects

The translational and clinical research on NGF has expanded the spectrum of diseases that could benefit from NGF treatment. This includes potential applications in Alzheimer’s disease, peripheral neuropathies, ocular and skin diseases, gliomas, traumatic brain injuries, vascular and immune diseases . Innovative delivery strategies and additional pathologies to be treated are also being explored, offering promising avenues for future research and therapeutic development .

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