NT 3 Human

Neurotrophin-3 Human Recombinant
Cat. No.
BT11079
Source
Escherichia Coli.
Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec'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-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x119 amino acid chains, having a total Mw of 27.2 kDa.
The NT-3 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Neurotrophin-3 (NT-3) is a neurotrophic factor that belongs to the neurotrophin family, which also includes nerve growth factor (NGF) and brain-derived neurotrophic factor (BDNF). NT-3 is essential for the survival and differentiation of various neuronal populations in the developing and adult nervous system. It plays a crucial role in the development of sensory neurons, sympathetic neurons, and motor neurons. NT-3 exerts its biological effects by binding to and activating specific cell surface receptors, primarily TrkC (tropomyosin receptor kinase C) and p75NTR (p75 neurotrophin receptor).
Description
Recombinant Human Neurotrophin-3 is a non-glycosylated homodimer protein expressed in E. coli. It consists of two identical polypeptide chains, each containing 119 amino acids, with a total molecular weight of 27.2 kDa. The protein is purified using proprietary chromatographic techniques to ensure high purity and homogeneity.
Physical Appearance
Sterile, white, lyophilized (freeze-dried) powder.
Formulation
Lyophilized in a solution containing 0.02% trifluoroacetic acid (TFA).
Solubility
To reconstitute lyophilized Neurotrophin-3, it is recommended to dissolve the powder in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. The reconstituted solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized NGF2, while stable at room temperature for up to 3 weeks, should ideally be stored desiccated at a temperature below -18°C. Once reconstituted, NGF-2 can be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store the reconstituted protein at -18°C with the addition of a carrier protein such as 0.1% HSA or BSA to enhance stability. Avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of Neurotrophin-3 is greater than 97.0%, as determined by two independent methods: reverse-phase high-performance liquid chromatography (RP-HPLC) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
Biological Activity
The biological activity of Neurotrophin-3 is measured by its ability to stimulate the proliferation of C6 cells in a dose-dependent manner. The ED50, which represents the concentration of NT-3 required to achieve half-maximal proliferation, is typically in the range of 3.6-5.4 µg/ml.
Protein Content
The protein content of Neurotrophin-3 is determined using two independent methods: (1) UV spectroscopy at 280 nm, employing an absorbance value of 2.165 as the extinction coefficient for a 0.1% (1 mg/ml) solution, calculated using the PC GENE computer analysis program; and (2) RP-HPLC analysis, utilizing a standard solution of NT-3 as a reference standard.
Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Source
Escherichia Coli.
Amino Acid Sequence
YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

Product Science Overview

Structure and Function

NT-3 is a protein that is highly conserved across species, with identical amino acid sequences in humans, mice, and pigs . It exists as a monomer with a molecular weight of approximately 13.6 kDa or as a dimer with a molecular weight of 27.2 kDa . The protein is involved in the development and maintenance of neuronal populations and promotes the differentiation of neural crest-derived sensory and sympathetic neurons .

Biological Activity

NT-3 exerts its effects by binding to and activating specific receptors on the surface of target cells. It primarily interacts with the TrkC receptor but can also bind to TrkA and TrkB receptors . Upon binding, these receptors activate several intracellular signaling pathways, including the Ras/MAPK pathway, the PI3 kinase/Akt pathway, and the PLC-γ1/PKC pathway . These pathways are involved in promoting neuronal differentiation, survival, growth, and synaptic plasticity .

Expression and Role in Development

NT-3 is expressed in various cell types, including neuronal cells, eosinophils, and melanocytes . It is essential for the development of peripheral sensory neurons and is required for the proper functioning of the nervous system . Knock-out studies in mice have shown that the absence of NT-3 leads to movement and posture deficiencies due to proprioception defects and loss of neurons in spinal and cephalic sensory ganglia .

Recombinant Human NT-3

Recombinant human NT-3 (hNT-3) is produced using recombinant DNA technology, typically in bacterial systems such as E. coli . The recombinant protein is purified to high levels of purity, often greater than 95% . It is used in various research applications to study its effects on neuronal cells and to understand its role in the nervous system.

Recombinant hNT-3 is supplied in a lyophilized form and can be reconstituted with sterile water or buffer solutions . It is stable at -20°C for long-term storage and can be used in various experimental setups to study its biological activity .

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