SEPX1 Human

Selenoprotein X 1 Human Recombinant
Cat. No.
BT21816
Source
Escherichia Coli.
Synonyms
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
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

SEPX1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Methionine sulfoxide reductase B1 (SEPX1 or MSRB1) is a selenoprotein crucial for reducing oxidized methionine (methionine sulfoxide) back to methionine. It specifically targets the R-isomer of methionine sulfoxide. Found in various tissues, SEPX1 belongs to the methionine sulfoxide reductase B family and utilizes a selenocysteine residue at its active site for its catalytic activity. The oxidation of methionine, primarily by reactive oxygen species, results in two forms of methionine sulfoxide, Met-S-SO and Met-R-SO. These forms are addressed by two distinct enzyme families: MsrA (methionine-S-sulfoxide reductase), specific to Met-S-SO, and MsrB (methionine-R-sulfoxide reductase), specific to Met-R-SO.
Description
This product consists of a recombinant human SEPX1 protein with a 20 amino acid His tag attached to its N-terminus. Produced in E. coli, this non-glycosylated polypeptide chain contains 136 amino acids (1-116 a.a.) and has a molecular weight of 14.8kDa. Due to the presence of selenocysteine (Sec/U) directly after the UGA codon in bacterial selenoproteins, the Sec-95 residue has been mutated to Cys. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
A clear and sterile solution.
Formulation
The SEPX1 solution is provided at a concentration of 0.5 mg/ml in a buffer containing 20mM Tris-HCl (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA, and 10% Glycerol.
Stability
For optimal storage, keep the vial at 4°C if it will be fully used within 2-4 weeks. For long-term storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is suggested for extended storage. Minimize repeated freeze-thaw cycles.
Purity
The purity of this product is greater than 90% as assessed by SDS-PAGE.
Synonyms
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFCIFSSS LKFVPKGKET SASQGH.

Product Science Overview

Introduction

Selenoprotein X 1 (SelX1) is a member of the selenoprotein family, which are proteins that incorporate selenium in the form of the amino acid selenocysteine. Selenium is an essential trace element known for its role in various biological processes, including antioxidant defense, thyroid hormone metabolism, and immune function .

Structure and Function

Selenoprotein X 1 is characterized by the presence of a selenocysteine residue at its active site. This residue is encoded by the UGA codon, which typically signals the end of protein synthesis but is recoded to incorporate selenocysteine in selenoproteins. The unique properties of selenocysteine, including its high reactivity and ability to participate in redox reactions, contribute to the functional diversity of selenoproteins .

Biological Role

The exact biological function of Selenoprotein X 1 is still under investigation. However, like other selenoproteins, it is believed to play a role in protecting cells from oxidative damage. Selenoproteins are known to be involved in redox homeostasis, and their antioxidant properties help mitigate the effects of reactive oxygen species (ROS) and other free radicals .

Expression and Regulation

The expression of Selenoprotein X 1, like other selenoproteins, is regulated by selenium availability. In conditions of selenium deficiency, the synthesis of selenoproteins is prioritized based on their importance to cellular function. This hierarchical regulation ensures that essential selenoproteins are synthesized even when selenium levels are low .

Recombinant Production

Human recombinant Selenoprotein X 1 is produced using recombinant DNA technology. This involves inserting the gene encoding SelX1 into a suitable expression system, such as bacteria or yeast, which then produces the protein. Recombinant production allows for the study of SelX1 in vitro and facilitates research into its structure, function, and potential therapeutic applications .

Potential Applications

Research into Selenoprotein X 1 and other selenoproteins holds promise for various medical applications. Understanding the role of SelX1 in redox biology and its potential protective effects against oxidative stress could lead to new therapeutic strategies for diseases associated with oxidative damage, such as neurodegenerative disorders, cardiovascular diseases, and cancer .

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