Recombinant Human GNAI3 Protein

Name: Recombinant Human GNAI3 Protein
Brand: Beta LifeScience
SKU: BL-0388SG
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	GST
Host Species	Human
Accession	NM_006496
Synonym	87U6; ARCND1
Background	Guanine nucleotide-binding proteins (G proteins) are heterotrimeric signal-transducing molecules consisting of alpha, beta, and gamma subunits, and function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha subunit binds guanine nucleotide, can hydrolyze GTP, and can interact with other proteins. G protein subunit alpha i3 (GNAI3) stimulates the activity of receptor-regulated K+ channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.
Description	Recombinant human GNAI3 (2-end) was produced in E. coli, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods. This protein is purified with our unique purification methods.
Source	E.coli
AA Sequence	2a.a.-end
Molecular Weight	65 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Active
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human GNAI3 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.
Subcellular Location	Cytoplasm. Cell membrane; Lipid-anchor. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	G-alpha family, G(i/o/t/z) subfamily
Database References	HGNC: 4387 OMIM: 139370 KEGG: hsa:2773 STRING: 9606.ENSP00000358867 UniGene: Hs.73799
Associated Diseases	Auriculocondylar syndrome 1 (ARCND1)

Gene Functions References

magnetic field-dependent nuclear magnetic resonance relaxation analyses were used to investigate the structural and dynamic properties of GDP bound Galpha on a microsecond timescale. PMID: 28223697
Results show that Galphai3 nuclear translocation causes irradiation resistance in human glioma cells through its complexation with DNA-PKcs leading to DNA repair. PMID: 28456783
GNAI3 is identified a second gene possibly responsible for X-linked ocular albinism. PMID: 27607449
Data show that auriculo-condylar syndrome (ACS)-associated mutations in G protein subunit alpha i3 (GNAI3) produce dominant-negative Galpha(i3) mutant proteins that couple to endothelin type A receptor (ET(A)R). PMID: 27072656
In postmortem human prefrontal cortex, adenosine A1 receptor is coupled preferentially, if not exclusively, to Galphai-3. PMID: 26213104
transcriptional upregulation of Girdin expression and Girdin-Galphai3 signaling play crucial roles in regulating epithelial apicobasal polarity through the PAR complex. PMID: 25977476
GIV and its substrate Galphai3 are recruited to active integrin complexes PMID: 26391662
We demonstrate that the GNAI3 variant is the likely cause of auriculocondylar syndrome in the original ACS1 family. PMID: 25026904
Both SH2 and GEF domains of GIV are required for the formation of a ligand-activated ternary complex between GIV, Galphai3, and EGFR. PMID: 25187647
Low GNAI3 expression is associated with hepatocellular carcinoma. PMID: 25444921
Data indicate that dynein- and astral microtubule-mediated transport of Galphai/LGN/nuclear mitotic apparatus (NuMA) complex from cell cortex to spindle poles. PMID: 23389635
The phenotypic variability of auriculocondylar syndrome suggests that mutations in this pathway, especially those affecting core signaling molecules such as PLCB4 and GNAI3, should be considered as potential candidates for other ear and jaw malformations. PMID: 22560091
These results identify the Oa1 transducer Galphai3 as the first downstream component in the Oa1 signaling pathway. PMID: 21931697
The mechanisms of regulation of GIRK by Galpha(i/o) using wild-type Galpha(i3) (Galpha(i3)WT) and Galpha(i3), were investigated. PMID: 21795707
These results provide mechanistic insights into how reversible modulation of Galpha(i3) activity by AGS3 and GIV maintains the delicate equilibrium between promotion and inhibition of autophagy. PMID: 21209316
Data suggest that Galphai-TNFAIP8-mediated rescue of pre-oncogenic cells enhances progression to oncogenic transformation, providing a selective target to inhibit cellular transformation. PMID: 20607800
we show that A3 adenosine receptor/Gi3 play important roles in human mast cells responses initiated on contact with activated T cells. PMID: 20190146
These data present AGS3, G-proteins, and mInsc as candidate proteins involved in regulating cellular stress associated with protein-processing pathologies. PMID: 20065032
Overexpression of GIPN stimulates proteasome-dependent reduction of endogenous G alpha i3 in HEK293 cells and reduces the half-life of overexpressed G alpha i3-YFP. PMID: 12826607
diffraction data were collected to 2.5 A resolution at 100 K using synchrotron radiation at Pohang beamline 4A for human RGS10 complexed with Galphai3 [Galphai3] PMID: 16511171
x-ray crystallography of the complex of RGS5 and Galphai(3) proteins with GDP/Mg(2+)/AlF(4)(-) at 3.0 A resolution PMID: 17100651
The Galphai3-GIV switch serves to link direction sensing from different families of chemotactic receptors to formation of the leading edge during cell migration. PMID: 18663145
Insulin-like growth factor-binding protein-5 stimulates growth of human intestinal muscle cells by activation of Galphai3. PMID: 19808657

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.