ARF5 Human

ADP-Ribosylation Factor 5 Human Recombinant
Cat. No.
BT13105
Source
Escherichia Coli.
Synonyms
ADP-ribosylation factor 5, ARF5.
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

ARF5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (1-180 a.a) and having a molecular mass of 22.6kDa.
ARF5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
As a small GTPase, ADP-ribosylation factor 5 (ARF5) plays a vital role in cellular processes by cycling between its active GTP-bound and inactive GDP-bound forms. It is known to stimulate the enzymatic activity of cholera toxin. ARF5 participates in various regulatory mechanisms, including the coordination of spectrin interactions with Golgi membranes and linking actin to the Golgi apparatus through Rho GTPase-dependent localization and WASP/Arp2/3 complexes. Notably, ARF5 contributes to vesicular transport and function by activating phospholipase D.
Description
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.
Physical Appearance
The product is provided as a sterile, colorless solution.
Formulation
The ARF5 protein is supplied in a solution containing 1 mg/ml ARF5, 20 mM Tris-HCl buffer (pH 8.0), 1 mM DTT, 20% glycerol, and 0.1 M NaCl.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the protein at -20°C. To further enhance long-term stability, the addition of a carrier protein like HSA or BSA (0.1%) is advisable. It is important to avoid repeated freeze-thaw cycles to maintain protein integrity.
Purity
The purity of the ARF5 protein is determined to be greater than 90% using SDS-PAGE analysis.
Synonyms
ADP-ribosylation factor 5, ARF5.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGLTVSALFS RIFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV QESADELQKM LQEDELRDAV LLVFANKQDM PNAMPVSELT DKLGLQHLRS RTWYVQATCA
TQGTGLYDGL DWLSHELSKR.

Product Science Overview

Gene Family and Classification

The ARF gene family consists of six ARF proteins and eleven ARF-like proteins, all of which belong to the RAS superfamily. The ARF proteins are categorized into three classes:

  • Class I: ARF1, ARF2, ARF3
  • Class II: ARF4, ARF5
  • Class III: ARF6

Each class shares a common gene organization, and the ARF5 gene spans approximately 3.2 kb of genomic DNA, containing six exons and five introns .

Function and Mechanism

ARF5 is involved in protein trafficking, particularly in modulating vesicle budding and uncoating within the Golgi apparatus. It functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase . This activation is crucial for the toxin’s ability to modify host cell proteins, leading to various cellular responses.

Cellular Localization and Expression

ARF5 is primarily localized in the cytoplasm, perinuclear region, plasma membrane, and Golgi apparatus. It is also found in extracellular exosomes . The gene is expressed in various tissues, including the prefrontal cortex, skin, pancreas, and cerebellum .

Interactions and Pathways

ARF5 interacts with several proteins, including ARFIP2, and is involved in multiple cellular pathways such as:

  • Vesicle-mediated transport
  • Golgi-to-ER retrograde transport
  • Intracellular protein transport

These interactions and pathways highlight the importance of ARF5 in maintaining cellular homeostasis and facilitating efficient protein trafficking .

Clinical Relevance

Mutations or dysregulation of ARF5 have been associated with diseases such as cholera and congenital myasthenic syndrome . Understanding the function and regulation of ARF5 can provide insights into the molecular mechanisms underlying these conditions and potentially lead to the development of targeted therapies.

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