Recombinant Proteins

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ARF1 Human

ADP-Ribosylation Factor 1 Human Recombinant

This product consists of Recombinant Human ARF1, a single, non-glycosylated polypeptide chain produced in E. coli. It encompasses 201 amino acids, including a 20 amino acid His-Tag fused at the N-terminus, resulting in a molecular mass of 22.8 kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12908
Source
Escherichia Coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized through filtration.

ARF3 Human

ADP-Ribosylation Factor 3 Human Recombinant

Recombinant Human ARF3, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) with a molecular weight of 22.8 kDa. ARF3 is fused to a 20 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT12963
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

ARF4 Human

ADP-Ribosylation Factor 4 Human Recombinant

Recombinant human ARF4, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 23kDa. It comprises 204 amino acids, including a 24 amino acid His tag at the N-terminus (1-180 a.a.). Purification of ARF4 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13043
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

ARF5 Human

ADP-Ribosylation Factor 5 Human Recombinant

Recombinant ARF5, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing 200 amino acids (including a 20 amino acid His-tag at the N-terminus). It has a molecular weight of 22.6 kDa. The protein is purified using proprietary chromatographic methods to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT13105
Source
Escherichia Coli.
Appearance
The product is provided as a sterile, colorless solution.

ARF6 Human

ADP-Ribosylation Factor 6 Human Recombinant

Recombinant ARF6, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 195 amino acids (1-175a.a.) with a molecular weight of 22.2 kDa. It includes a 20 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT13194
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

ARL2BP Human

ADP-Ribosylation Factor-Like 2 Binding Protein Human Recombinant

Recombinant human ARL2BP, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 183 amino acids (residues 1-163) with a molecular weight of 20.9 kDa. It includes a 20 amino acid His-Tag at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13994
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ARL3 Human

ADP-Ribosylation Factor-Like 3 Human Recombinant

Recombinant human ARL3 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It contains 206 amino acids (including a 24 amino acid His-tag at the N-terminus) and has a molecular weight of 23kDa. The protein sequence comprises amino acids 1-182 of the ARL3 protein, with an additional His-tag for purification. ARL3 is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14132
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

ARL4A Human

ADP-Ribosylation Factor-Like 4A Human Recombinant

Recombinantly produced in E.coli, ARL4A Human is a single, non-glycosylated polypeptide chain consisting of 220 amino acids (1-200) with a molecular weight of 24.7 kDa. This protein features a 20 amino acid His-Tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14222
Source
E.coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

ARL11 Human

ADP-Ribosylation Factor-Like 11 Human Recombinant

Recombinant human ARL11, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 216 amino acids (specifically, amino acids 1-196). It has a molecular weight of 23.6 kDa. This ARL11 protein is fused to a 20 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13641
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

ARL14 Human

ADP-Ribosylation Factor-Like 14 Human Recombinant

Recombinant ARL14 Human, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 212 amino acids (residues 1-192) and possesses a molecular mass of 23.8 kDa. It's important to note that the molecular weight on SDS-PAGE will appear higher. This protein is engineered with a 20 amino acid His-tag fused at the N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT13753
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Definition and Classification

ADP-Ribosylation Factors (ARFs) are small GTP-binding proteins that belong to the Ras superfamily. They play a crucial role in regulating vesicular traffic and actin remodeling. ARFs are ubiquitous in eukaryotic cells, with six highly conserved members identified in mammalian cells . These proteins cycle between inactive GDP-bound and active GTP-bound forms, binding selectively to effectors .

Biological Properties

Key Biological Properties: ARFs are involved in various cellular processes, including vesicle biogenesis and intracellular traffic . They are generally associated with membranes due to N-terminus myristoylation .

Expression Patterns and Tissue Distribution: ARFs are expressed ubiquitously across different tissues. They are particularly abundant in tissues with high vesicular traffic activity, such as the Golgi apparatus .

Biological Functions

Primary Biological Functions: ARFs regulate membrane trafficking pathways, including secretion, endocytosis, and phagocytosis . They also play a role in cell adhesion and tumor-cell invasion .

Role in Immune Responses and Pathogen Recognition: ARFs are involved in immune responses by regulating the trafficking of immune receptors and signaling molecules .

Modes of Action

Mechanisms with Other Molecules and Cells: ARFs interact with various proteins, including coat proteins and lipid-modifying enzymes . They function as regulatory subunits controlling coat assembly in vesicles .

Binding Partners and Downstream Signaling Cascades: ARFs bind to guanosine nucleotides (GTP and GDP) and undergo conformational changes that propagate structural information . These changes affect downstream signaling pathways involved in vesicle formation and trafficking .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: ARFs are regulated by GTPase-activating proteins (GAPs) and guanine nucleotide-exchange factors (GEFs), which facilitate the exchange of GDP for GTP . Post-translational modifications, such as myristoylation, also play a role in their regulation .

Transcriptional Regulation and Post-Translational Modifications: ARFs undergo various post-translational modifications, including phosphorylation and ubiquitination, which modulate their activity and stability .

Applications

Biomedical Research: ARFs are studied for their role in vesicular trafficking and their potential involvement in diseases such as cancer and neurodegeneration .

Diagnostic Tools and Therapeutic Strategies: ARFs are potential targets for therapeutic interventions aimed at modulating vesicular traffic in disease conditions .

Role in the Life Cycle

Role Throughout the Life Cycle: ARFs are involved in various stages of the cellular life cycle, from development to aging . They play a role in DNA repair, transcriptional regulation, and cell cycle control . Dysregulation of ARF activity has been linked to diseases such as cancer and neurodegeneration .

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