Recombinant Human Adp-Ribosylation Factor-Like Protein 2 (ARL2) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08513P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Adp-Ribosylation Factor-Like Protein 2 (ARL2) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08513P
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Product Overview

Description Recombinant Human Adp-Ribosylation Factor-Like Protein 2 (ARL2) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P36404
Target Symbol ARL2
Synonyms ADP ribosylation factor like 2; ADP-ribosylation factor-like protein 2; ARFL2; Arl184; Arl2; ARL2_HUMAN
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence LLMLGLDNAGKTTILKKFNGEDIDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSSNAIREVLELDSIRSHHWCIQGCSAVTGENLLPGIDWLLDDISSRIFTAD
Expression Range 19-184aa
Protein Length Partial
Mol. Weight 45.7kDa
Research Area Cell Cycle
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function 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 Ca(2+)-dependent release of acetylcholine. Required for normal progress through the cell cycle. Also regulates mitochondrial integrity and function.
Subcellular Location Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm.
Protein Families Small GTPase superfamily, Arf family
Database References

HGNC: 693

OMIM: 601175

KEGG: hsa:402

STRING: 9606.ENSP00000246747

UniGene: PMID: 29265919

  • conclude that the TBCD*ARL2*beta-tubulin complex represents a functional intermediate in the beta-tubulin folding pathway whose activity is regulated by the cycling of nucleotides on ARL2 PMID: 28970104
  • Results identified ARL2 and TBCD, as important in tubulin folding and microtubule dynamics. Both ARL2 and TBCD also localize to centrosomes. A growing body of evidence also has found roles for ARL2 inside mitochondria, as a regulator of mitochondrial fusion, and in the traffic of farnesylated cargos between membranes and specifically to cilia and photoreceptor cells. [review] PMID: 27400436
  • In conclusion, our study revealed that miR-214 acts as a tumor suppressor via inhibiting proliferation, migration and invasion of cervical cancer cells through targeting ARL2, and that both miR-214 and ARL2 may serve as prognostic or therapeutic targets for cervical cancer. PMID: 28137590
  • Novel Biochemical and Structural Insights into the Interaction of Myristoylated Cargo with Unc119 Protein and Their Release by Arl2/3. PMID: 27481943
  • We hypothesize that ARL2 plays essential roles inside mitochondria along with other cellular functions, at least in part to provide coupling of regulation between these essential cell processes. PMID: 24911211
  • MiR-195 regulates cell apoptosis in a context-dependent manner through directly targeting ARL2. PMID: 23807224
  • The G proteins Arl2 acts in a GTP-dependent manner as allosteric release factors for farnesylated cargo. PMID: 22002721
  • a novel function of miR-16 targeting ARL2 in modulating proliferation and cell cycle progression. PMID: 21199864
  • Data show that bovine and human TBCD have functionally identical roles in tubulin heterodimer assembly, and that the inability of human TBCD to disrupt microtubule integrity can be overcome by siRNA-mediated suppression of expression of Arl2. PMID: 20740604
  • C. elegans evl-20 gene encodes a functional homolog of human ARL2. Elimination of evl-20 function results in abnormal vulval, gonad, and male tail development and disrupts embryonic proliferation, hypodermal enclosure, and elongation. PMID: 12015966
  • Arl2 is present in centrosomes and propose that its action in regulating tubulin polymerization is mediated at centrosomes PMID: 16525022
  • In summary, alterations in Arl2 protein content were found to be associated with modifications in tubulin pools, microtubule dynamics as well as cell cycle progression. PMID: 17188265
  • ARL2 and beta-tubulin cofactor D participate in AJC disassembly and epithelial depolarization PMID: 17704193
  • Arl2 and Arl3 interactions were characterized. PMID: 18588884
  • Arl2 could, via protein phosphatase 2A , influence p53 phosphorylation status. PMID: 18818514
  • Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector. PMID: 19368893
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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