Recombinant Proteins

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sRAGE Human

Advanced Glycosylation End Product-Specific Receptor Human Recombinant

Recombinant Human sRAGE, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 339 amino acids, resulting in a molecular weight of 36.5 kDa. This sRAGE protein features a 14-amino acid His tag fused at its N-terminus and is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT2656
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder.

sRAGE Mouse

Advanced Glycosylation End Product-Specific Receptor Mouse Recombinant

Recombinant sRAGE Mouse, produced in HEK cells, is a single, glycosylated polypeptide chain containing 317 amino acids (Gly23-Asp333). It has a molecular mass of 34.0 kDa. sRAGE Mouse is fused to a 6 a.a his tag at the C-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2725
Source

HEK 293.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

RAGE Human, Sf9

Advanced Glycosylation End Product-Specific Receptor Human Recombinant, Sf9

This product consists of the extracellular domain (amino acids 24-342) of human RAGE, produced in Sf9 insect cells. It is a single, glycosylated polypeptide chain with a C-terminal His-tag fused to a human IgG domain. The molecular weight is 61.2 kDa, and purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT2496
Source

Sf9, Baculovirus cells.

Appearance
A clear and colorless solution after sterile filtration.
Definition and Classification

The soluble receptor for advanced glycation end products (sRAGE) is a variant of the receptor for advanced glycation end products (RAGE). RAGE is a transmembrane receptor of the immunoglobulin superfamily, primarily known for binding advanced glycation end products (AGEs). sRAGE, however, is a soluble form that lacks the transmembrane and cytoplasmic domains, allowing it to circulate freely in the bloodstream. It is generated either through alternative splicing of the RAGE gene or by proteolytic cleavage of the membrane-bound RAGE (mRAGE) .

Biological Properties

Key Biological Properties: sRAGE acts as a decoy receptor, binding to AGEs and other ligands, thereby preventing them from interacting with cell surface RAGE and triggering inflammatory responses .

Expression Patterns and Tissue Distribution: sRAGE is predominantly expressed in endothelial cells, but it is also found in various other tissues, including the lungs, kidneys, and heart . Its levels can vary significantly depending on the physiological and pathological conditions of the body .

Biological Functions

Primary Biological Functions: sRAGE plays a crucial role in modulating inflammatory responses by sequestering ligands that would otherwise bind to mRAGE and activate pro-inflammatory signaling pathways .

Role in Immune Responses and Pathogen Recognition: sRAGE is involved in the immune response by acting as a pattern recognition receptor (PRR). It binds to various ligands, including AGEs, high mobility group box 1 (HMGB1), and S100 proteins, which are associated with inflammation and immune responses .

Modes of Action

Mechanisms with Other Molecules and Cells: sRAGE interacts with multiple ligands, including AGEs, HMGB1, and S100 proteins. By binding these ligands, sRAGE prevents them from interacting with mRAGE, thereby inhibiting downstream pro-inflammatory signaling cascades .

Binding Partners and Downstream Signaling Cascades: The binding of sRAGE to its ligands inhibits the activation of several signaling pathways, including the nuclear factor kappa B (NF-κB) pathway, which is crucial for the expression of pro-inflammatory cytokines . This inhibition helps in reducing inflammation and oxidative stress .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression of sRAGE is regulated at both the transcriptional and post-transcriptional levels. Transcriptional regulation involves various transcription factors that bind to the promoter region of the RAGE gene . Post-translational modifications, such as glycosylation and proteolytic cleavage, also play a significant role in the generation and activity of sRAGE .

Applications

Biomedical Research: sRAGE is extensively studied as a biomarker for various diseases, including diabetes, cardiovascular diseases, and chronic inflammatory conditions .

Diagnostic Tools: Measuring circulating levels of sRAGE can help in diagnosing and predicting the prognosis of diseases associated with chronic inflammation and oxidative stress .

Therapeutic Strategies: sRAGE is being explored as a potential therapeutic agent to treat inflammatory diseases by acting as a decoy receptor to neutralize the effects of pro-inflammatory ligands .

Role in the Life Cycle

Role Throughout the Life Cycle: sRAGE plays a significant role throughout the life cycle, from development to aging. During development, it helps in modulating inflammatory responses, which is crucial for proper tissue formation and function . In aging and disease, sRAGE levels are often altered, contributing to the pathogenesis of various age-related diseases, including atherosclerosis, diabetes, and neurodegenerative disorders .

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