MTPN Human

Myotrophin Human Recombinant
Cat. No.
BT12022
Source
Escherichia Coli.
Synonyms
Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% 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

MTPN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 15 kDa. The MTPN is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Myotrophin (MTPN) is an ankyrin repeat protein that promotes cardiac hypertrophy. It achieves this by stimulating protein synthesis and cardiomyocyte growth, ultimately activating the NF-kappaB signaling cascade. MTPN also plays a crucial role in cerebellar development, contributing to its morphogenesis and the differentiation of cerebellar neurons, particularly granule cells. Elevated levels of MTPN are observed in individuals with dilated cardiomyopathy and ischemic heart conditions.
Description
Recombinant Human MTPN, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 138 amino acids, with 118 amino acids forming the MTPN sequence (1-118 a.a.) and a 20 amino acid His-Tag at the N-terminus. This protein has a molecular weight of 15 kDa and is purified using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for clarity.
Formulation
The formulation for Human MTPN consists of a solution containing 20mM Tris-HCl at pH 8 and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For long-term storage, it is recommended to freeze the product at -20°C. To ensure stability during long-term storage, consider adding a carrier protein such as 0.1% HSA or BSA. Avoid repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
Protein V-1, GCDP, Myotrophin, FLJ31098, FLJ99857.
Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ.

Product Science Overview

Structure and Expression

Myotrophin is composed of 118 amino acids and has a molecular weight of approximately 15 kDa . The protein is typically expressed in Escherichia coli (E. coli) for recombinant production . The recombinant form of Myotrophin often includes a His-tag at the N-terminus to facilitate purification and detection .

Biological Functions
  1. Cardiac Hypertrophy: Myotrophin is known to stimulate protein synthesis and cardiomyocyte growth, which leads to cardiac hypertrophy. This process is mediated through the activation of the NF-kappaB signaling cascade . Elevated levels of Myotrophin have been observed in human dilated cardiomyopathic and ischemic hearts .

  2. Cerebellar Morphogenesis: Myotrophin plays a potential role in the development of the cerebellum, particularly in the differentiation of cerebellar neurons such as granule cells .

  3. Skeletal Muscle Growth: In addition to its role in cardiac and neural tissues, Myotrophin has been shown to promote skeletal muscle growth both in vitro and in vivo .

Applications and Research

Recombinant Myotrophin is widely used in research to study its various functions and potential therapeutic applications. It is utilized in experiments involving SDS-PAGE and mass spectrometry to analyze its purity and molecular weight . The protein is also used in studies focusing on cardiac hypertrophy, neurogenesis, and muscle differentiation.

Storage and Stability

Recombinant Myotrophin is typically shipped and stored at 4°C for short-term use (1-2 weeks). For long-term storage, it is aliquoted and kept at -20°C or -80°C to avoid freeze-thaw cycles, which can degrade the protein .

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