Recombinant Proteins

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RGS2 Human

Regulator of G-Protein Signaling 2 Human Recombinant

Produced in E. coli, RGS2 is a single, non-glycosylated polypeptide chain with 231 amino acids (1-211a.a.) and a molecular weight of 26.5 kDa. This protein consists of amino acids 1-211 and includes a 20 amino acid His-tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12838
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

RGS21 Human

Regulator of G-Protein Signaling 21 Human Recombinant

Recombinant Human RGS21, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 176 amino acids (residues 1-152) with a molecular weight of 20.2 kDa. It includes a 24-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12918
Source
Escherichia Coli.
Appearance
Clear, colorless and sterile filtered solution.

RGS4 Human

Regulator of G-Protein Signaling 4 Human Recombinant

This product consists of a recombinant human RGS4 protein produced in E. coli. It is a single, non-glycosylated polypeptide chain comprising 225 amino acids (specifically, amino acids 1 to 205) with a molecular weight of 25.4 kDa. For purification and detection purposes, the RGS4 protein has a 20 amino acid His-tag fused to its N-terminus. The purification process utilizes proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT13023
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.

RGS5 Human

Regulator of G-Protein Signaling 5 Human Recombinant

Recombinant human RGS5, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 205 amino acids (1-181 a.a.) with a molecular weight of 23.5 kDa. This protein is designed with a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13112
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

RGS1 Human

Regulator of G-Protein Signaling 1 Human Recombinant

Recombinant human RGS1, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 233 amino acids (residues 1-209). With a molecular mass of 26 kDa, it includes a 24 amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12369
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

RGS10 Human

Regulator of G-Protein Signaling 10 Human Recombinant

Recombinant RGS10, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 205 amino acids (residues 1-181). With a molecular weight of 23.7 kDa, it features a 24 amino acid His-Tag fused to its N-terminus. This protein has been purified using proprietary chromatographic techniques to ensure its high quality and purity.
Shipped with Ice Packs
Cat. No.
BT12451
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

RGS14 Human

Regulator of G-Protein Signaling 14 Human Recombinant

Recombinant Human RGS14, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 586 amino acids (specifically, amino acids 1-566) and exhibits a molecular weight of 63.6kDa. The protein is engineered with a 20 amino acid His-tag at its N-terminus and purified using specialized chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12530
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized by filtration.

RGS16 Human

Regulator of G-Protein Signaling 16 Human Recombinant

Recombinant human RGS16, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 222 amino acids (residues 1-202) with a molecular weight of 24.9 kDa. A 20 amino acid His Tag is fused to the N-terminus of the protein, which is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12602
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

RGS17 Human

Regulator of G-Protein Signaling 17 Human Recombinant

Recombinant human RGS17 is produced in E. coli as a non-glycosylated polypeptide chain. It consists of 230 amino acids (residues 1-210) and has a molecular mass of 26.5 kDa. The protein includes a 20-amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT12673
Source
E.coli.
Appearance
Colorless, sterile filtered solution.

RGS19 Human

Regulator of G-Protein Signaling 19 Human Recombinant

Recombinant RGS19, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 1 to 217. It possesses a molecular weight of 26.7 kDa, including a 20 amino acid His-tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12768
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.
Definition and Classification

Regulators of G-Protein Signaling (RGS) are protein structural domains or proteins containing these domains that function to activate the GTPase activity of heterotrimeric G-protein α-subunits . RGS proteins are multi-functional, GTPase-accelerating proteins that promote GTP hydrolysis by the α-subunit of heterotrimeric G proteins, thereby inactivating the G protein and rapidly switching off G protein-coupled receptor (GPCR) signaling pathways . RGS proteins have been conserved throughout evolution and are classified into several subfamilies based on their structural domains and functions .

Biological Properties

Key Biological Properties: RGS proteins are characterized by their ability to accelerate GTP hydrolysis, thus inactivating G proteins . They contain an RGS-box (or RGS domain), which is essential for their activity .

Expression Patterns and Tissue Distribution: RGS proteins are expressed in various tissues and cells, including the brain, heart, and immune cells . Their expression patterns can vary significantly, with some RGS proteins being ubiquitously expressed while others are tissue-specific .

Biological Functions

Primary Biological Functions: The primary function of RGS proteins is to regulate GPCR signaling by accelerating the GTPase activity of Gα subunits . This leads to the termination of GPCR downstream signaling pathways .

Role in Immune Responses and Pathogen Recognition: RGS proteins play crucial roles in immune responses by modulating the signaling pathways involved in immune cell activation and migration . They are also involved in pathogen recognition and the regulation of inflammatory responses .

Modes of Action

Mechanisms with Other Molecules and Cells: RGS proteins interact with Gα subunits of heterotrimeric G proteins, promoting GTP hydrolysis and inactivating the G protein . This interaction is critical for the regulation of GPCR signaling .

Binding Partners and Downstream Signaling Cascades: RGS proteins can bind to various Gα subunits, and their activity is modulated by other proteins and post-translational modifications . They influence downstream signaling cascades by terminating GPCR signaling .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of RGS proteins are regulated at multiple levels, including transcriptional regulation and post-translational modifications . Transcription factors and signaling pathways can modulate the expression of RGS genes .

Transcriptional Regulation and Post-Translational Modifications: RGS proteins undergo various post-translational modifications, such as phosphorylation and ubiquitination, which can affect their stability and activity . These modifications play a crucial role in fine-tuning the activity of RGS proteins in response to cellular signals .

Applications

Biomedical Research: RGS proteins are valuable tools in biomedical research for studying GPCR signaling and its regulation . They are used to investigate the mechanisms of various diseases and to identify potential therapeutic targets .

Diagnostic Tools and Therapeutic Strategies: RGS proteins have potential applications in diagnostics and therapeutics. They can serve as biomarkers for certain diseases and as targets for drug development . Modulating the activity of RGS proteins could provide new therapeutic strategies for treating diseases associated with dysregulated GPCR signaling .

Role in the Life Cycle

Role Throughout the Life Cycle: RGS proteins play essential roles throughout the life cycle, from development to aging and disease . During development, they regulate cell signaling pathways that control cell proliferation, differentiation, and migration . In aging and disease, dysregulation of RGS protein activity can contribute to various pathological conditions, including cancer and neurodegenerative diseases .

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