ARL1 Human

ADP-Ribosylation Factor-Like 1 Human Recombinant
Cat. No.
BT13553
Source
Escherichia Coli.
Synonyms
ARFL1.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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

ARL1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (1-181 a.a.) and having a molecular mass of 22.5 kDa.
The ARL1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
ARL1, a member of the ARL protein family, shares structural similarities with ADP-ribosylation factors (ARFs). ARFs are known to activate cholera toxin (CT) ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform. ARL1 demonstrates weak stimulation of both PLD and CT in a phospholipid-dependent manner. As a GTP-binding protein, ARL1 exhibits low efficiency as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. ARL1 plays a role in the Golgi apparatus.
Description
Recombinant Human ARL1, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 201 amino acids (1-181 a.a.). With a molecular weight of 22.5 kDa, this protein features a 20 amino acid His-Tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The ARL1 solution is provided at a concentration of 0.25 mg/ml and contains 20mM Tris-HCl (pH 8.0), 2mM DTT, 100mM NaCl, and 40% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Minimize repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
ARFL1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGGFFSSIFS SLFGTREMRI LILGLDGAGK TTILYRLQVG EVVTTIPTIG FNVETVTYKN LKFQVWDLGG QTSIRPYWRC YYSNTDAVIY VVDSCDRDRI GISKSELVAM LEEEELRKAI LVVFANKQDM EQAMTSSEMA NSLGLPALKD RKWQIFKTSA TKGTGLDEAM EWLVETLKSR Q.

Product Science Overview

Introduction

ADP-Ribosylation Factor-Like 1 (ARL1) is a member of the ADP-ribosylation factor (ARF) family of GTP-binding proteins, which are part of the larger Ras superfamily. These proteins are ubiquitous in eukaryotic cells and play crucial roles in various cellular processes, including vesicular trafficking and actin cytoskeleton remodeling .

Structure and Function

ARL1 is a small GTPase that cycles between an inactive GDP-bound form and an active GTP-bound form. This cycling is essential for its function in recruiting several effectors, such as golgins, arfaptins, and ARF-GEFs, to the trans-Golgi network. These interactions modulate various functions at the Golgi complex, including cell polarity, innate immunity, and protein secretion .

The protein consists of 181 amino acids and has several binding sites for GTP and magnesium ions, which are crucial for its activity. The conformational changes between the GDP-bound and GTP-bound states are characterized by alterations in the switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly to GDP .

Biological Significance

ARL1 plays a significant role in maintaining the structure and function of the Golgi apparatus. It is involved in the retrograde transport at the trans-Golgi network, which is essential for the proper sorting and trafficking of proteins within the cell. Additionally, ARL1 has been implicated in various cellular processes, including the maintenance of insulin secretion from pancreatic beta cells .

Recombinant Production

The human recombinant form of ARL1 is produced using recombinant DNA technology. This involves cloning the ARL1 gene into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or yeast. The host cells are cultured under conditions that promote the expression of the recombinant protein, which is subsequently purified using various chromatographic techniques.

Applications

Recombinant ARL1 is used in various research applications to study its role in cellular processes and its interactions with other proteins. It is also used in structural studies to understand the conformational changes associated with its GTPase activity. Additionally, recombinant ARL1 can be used in drug discovery efforts to identify potential inhibitors or modulators of its activity.

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