NRG1 A Human

Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant
Cat. No.
BT9903
Source
Escherichia Coli.
Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
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
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

Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa.
NRG1-A is purified by proprietary chromatographic techniques.

Product Specs

Introduction
The Neuregulin/Heregulin family encompasses structurally related polypeptide growth factors originating from alternatively spliced genes (NRG1, NRG2, NRG3, and NRG4). Currently, over 14 soluble and transmembrane proteins are derived from the NRG1 gene. These isoforms undergo proteolytic processing of their extracellular domain, leading to the release of soluble growth factors. Among these isoforms are the heregulins (HRGs), glial growth factors (GGFs), and sensory and motor neuron-derived factor (SMDF). Notably, all these factors share Ig and EGF-like domains, enabling them to bind to ErbB3 and ErbB4 receptor tyrosine kinases. This binding triggers the heterodimerization of ErbB3 and ErbB4 with ErbB2, consequently activating intrinsic kinase activity and resulting in tyrosine phosphorylation. The NRG1 isoforms play a crucial role in inducing growth and differentiation in various cell types, including epithelial, neuronal, glial, and others.
Description
Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain), produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 65 amino acids. It has a molecular mass of 7.4 kDa. The purification of NRG1-A is achieved through proprietary chromatographic techniques.
Physical Appearance
White, sterile-filtered powder obtained through lyophilization (freeze-drying).
Formulation
Lyophilized from a 0.2 µm filtered solution in 20 mM phosphate buffer (PB), with a pH of 6.0 and 150 mM sodium chloride (NaCl).
Solubility
For reconstitution, it is advised to dissolve the lyophilized NRG1-A in sterile 18 MΩ-cm H₂O at a concentration of at least 100 µg/ml. Further dilutions can be made using other aqueous solutions.
Stability
While lyophilized NRG1-A remains stable at room temperature for up to 3 weeks, it's recommended to store it desiccated below -18°C. After reconstitution, NRG1-A should be stored at 4°C for 2-7 days. For long-term storage, keep it below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 97.0%, as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) analysis. (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis.
Biological Activity
The ED₅₀, determined through dose-dependent stimulation of human MCF-7 cell proliferation, is less than 40 ng/ml. This corresponds to a specific activity greater than 2.5 × 10⁴ units/mg.
Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
Source
Escherichia Coli.
Amino Acid Sequence
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.

Product Science Overview

Introduction

Neuregulin-1 (NRG1), also known as Heregulin, is a member of the neuregulin family of structurally related glycoproteins. These proteins are known for their role in cell signaling and interaction with the ErbB family of receptor tyrosine kinases. NRG1 is particularly significant due to its involvement in various biological processes, including neural development, cardiac function, and cancer progression.

Structure and Isoforms

NRG1 is produced through alternative splicing of the NRG1 gene, resulting in multiple isoforms. These isoforms can be broadly categorized into two main types based on their EGF-like domain: NRG1-alpha and NRG1-beta. The EGF-like domain is crucial for binding to ErbB receptors and initiating downstream signaling pathways .

Biological Functions

NRG1 plays a pivotal role in the development and function of the nervous system and heart. It is involved in the differentiation and proliferation of Schwann cells, which are essential for myelination in the peripheral nervous system . Additionally, NRG1 is critical for the development of the neuromuscular junction and the regulation of neurotransmitter receptor expression .

In the heart, NRG1 is essential for cardiac development and function. It promotes the survival, growth, and differentiation of cardiac cells, and is involved in the response to cardiac injury .

Mechanism of Action

NRG1 exerts its effects by binding to the ErbB family of receptors, specifically ErbB3 and ErbB4. Upon binding, these receptors dimerize and undergo autophosphorylation, activating various intracellular signaling pathways such as the PI3K/Akt and MAPK pathways . These pathways are involved in cell survival, proliferation, and differentiation.

Recombinant NRG1

Recombinant human NRG1-alpha (EGF domain) is produced using recombinant DNA technology. It is typically expressed in bacterial or mammalian cell systems and purified for research and therapeutic applications. The recombinant protein retains the biological activity of the native protein and is used in various studies to understand its role in cell signaling and disease .

Applications in Research and Medicine

Recombinant NRG1 is widely used in research to study its role in neural and cardiac development, as well as its involvement in cancer. It is also being explored as a potential therapeutic agent for neurodegenerative diseases, heart failure, and certain types of cancer .

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