ADP-ribosylation factor-like protein 2; ARFL2

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 90% by SDS-PAGE

Liquid. In 20 mM Tris-HCl Buffer (pH 8.0) containing 0.1 mM PMSF, 1mM DTT, 40% glycerol

0.25 mg/ml (determined by Bradford assay) (lot specific)

Can be stored at 4 degree C short term (1-2 weeks).
For long term storage, aliquot and store at -20 degree C or -70 degree C.
Avoid repeated freezing and thawing cycles.

Small volumes of ARL2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

ARL2 belongs to the ADP-ribosylation factor (ARF) family. This protein functions as a component of a secretory pathway that is involved in the Ca2-dependent release of acetylcholine. It plays a role in the folding of tubule proteins, thereby playing an important role in microtubule dynamics and cell cycle progression. unlike other members of the ARF family, ARL2 does not act as an activator of the catalytic subunit of cholera toxin. Recombinant human ARL2 protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography.

Signal Transduction

SDS-PAGE

23.0 kDa (204aa), confirmed by MALDI-TOF

ADP ribosylation factor like GTPase 2

ADP-ribosylation factor-like protein 2

ADP-ribosylation factor-like protein 2

This gene encodes a small GTP-binding protein of the RAS superfamily which functions as an ADP-ribosylation factor (ARF). The encoded protein is one of a functionally distinct group of ARF-like genes. [provided by RefSeq, Jul 2008]

Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catalytic subunit. Regulates formation of new microtubules and centrosome integrity. Prevents the TBCD-induced microtubule destruction. Participates in association with TBCD, in the disassembly of the apical junction complexes. Antagonizes the effect of TBCD on epithelial cell detachment and tight and adherens junctions disassembly. Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. Component of a regulated secretory pathway involved in Ca2+-dependent release of acetylcholine. Required for normal progress through the cell cycle.

Smith DF., et al. (2010) Mol Biochem Parasitol. 173 (2):123-31.; Dumontet C., et al (2009) PLoS One. 4 (10):e7478.

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