Recombinant Proteins

p53
LBP
CEA
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SEP15 Human

15 KDa Selenoprotein Human Recombinant

SEP15 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 160 amino acids (29-165 a.a) and having a molecular mass of 17.7kDa.
SEP15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21661
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

SEPW1 Human

Selenoprotein W 1 Human Recombinant

SEPW1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 11.8kDa. 
SEPW1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21743
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

SEPX1 Human

Selenoprotein X 1 Human Recombinant

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.
Shipped with Ice Packs
Cat. No.
BT21816
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Selenoproteins are a unique class of proteins that incorporate selenium in the form of the amino acid selenocysteine. This incorporation occurs co-translationally, meaning it happens during the process of protein synthesis. Selenocysteine is often referred to as the 21st amino acid due to its unique properties and the specific mechanisms required for its incorporation into proteins . Selenoproteins are classified based on their function and the presence of selenocysteine residues. Notable examples include glutathione peroxidases, thioredoxin reductases, and selenoprotein P .

Biological Properties

Selenoproteins exhibit a range of biological properties, primarily due to their role in redox reactions. They are highly expressed in tissues such as the liver, kidney, and brain . The expression patterns of selenoproteins are tightly regulated, and their tissue distribution varies significantly. For instance, selenoprotein P is predominantly found in the plasma and serves as a selenium transporter . Other selenoproteins, like glutathione peroxidases, are crucial for protecting cells from oxidative damage .

Biological Functions

The primary biological functions of selenoproteins include antioxidant defense, redox regulation, and thyroid hormone metabolism . They play a crucial role in immune responses by modulating the activity of immune cells and protecting them from oxidative stress . Selenoproteins are also involved in pathogen recognition and the regulation of inflammatory responses . For example, glutathione peroxidases neutralize reactive oxygen species, thereby preventing cellular damage during immune responses .

Modes of Action

Selenoproteins interact with various molecules and cells through their redox-active selenocysteine residues. These interactions often involve the formation and reduction of disulfide bonds, which are critical for maintaining cellular redox homeostasis . Selenoproteins like thioredoxin reductases participate in downstream signaling cascades by modulating the redox state of target proteins . Additionally, selenoprotein P acts as a selenium transporter, delivering selenium to tissues and maintaining selenium homeostasis .

Regulatory Mechanisms

The expression and activity of selenoproteins are regulated at multiple levels, including transcriptional and post-translational modifications . Transcriptional regulation involves specific response elements in the promoter regions of selenoprotein genes that respond to selenium levels . Post-translational modifications, such as phosphorylation and ubiquitination, further modulate the activity and stability of selenoproteins . The hierarchy of selenoprotein expression ensures that essential selenoproteins are prioritized during selenium deficiency .

Applications

Selenoproteins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . Their antioxidant properties make them valuable in studying oxidative stress-related diseases, such as cancer and neurodegenerative disorders . Selenoproteins are also used as biomarkers for selenium status and oxidative stress . Therapeutically, selenium supplementation has been explored for its potential to enhance immune function and protect against oxidative damage .

Role in the Life Cycle

Selenoproteins play vital roles throughout the life cycle, from development to aging and disease . During development, they are essential for brain development, thyroid hormone metabolism, and immune function . In adulthood, selenoproteins continue to protect against oxidative stress and support immune responses . As organisms age, the expression and activity of selenoproteins may decline, contributing to age-related diseases and decreased immune function . Selenium supplementation has been investigated as a strategy to mitigate these effects and promote healthy aging .

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