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AB132889

Recombinant Human GNAQ protein

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(1 Publication)

Recombinant Human GNAQ protein is a Human Full Length protein, in the 1 to 359 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

GAQ, GNAQ, Guanine nucleotide-binding protein G(q) subunit alpha, Guanine nucleotide-binding protein alpha-q

1 Images
SDS-PAGE - Recombinant Human GNAQ protein (AB132889)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human GNAQ protein (AB132889)

12.5% SDS-PAGE analysis of ab132889 stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

Tag free

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

P50148

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV","proteinLength":"Full Length","predictedMolecularWeight":"65.23 kDa","actualMolecularWeight":null,"aminoAcidEnd":359,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P50148","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

GNAQ also known as Guanine nucleotide-binding protein G(q) subunit alpha plays a role in cell signaling as a modulator or transducer in various transmembrane signaling systems. With a molecular weight of approximately 42 kDa GNAQ belongs to the Gq family of G proteins. It is widely expressed in human tissues such as the brain heart and placenta. The protein's main mechanism involves binding to GTP and GDP leading it to switch between inactive GDP-bound and active GTP-bound states.
Biological function summary

GNAQ influences multiple cell processes mediating the activation of phospholipase C-beta a critical enzyme in hydrolyzing phosphatidylinositol 45-bisphosphate (PIP2) to inositol trisphosphate and diacylglycerol. This action leads to the release of calcium ions from intracellular stores. GNAQ acts as part of a heterotrimeric G protein complex which requires coordination with beta and gamma subunits to achieve full functional capability. Its activity is critical for processes like cell proliferation and differentiation.

Pathways

GNAQ notably participates in the phosphoinositide signaling pathway and calcium signaling pathway. In the phosphoinositide signaling pathway GNAQ facilitates the link between G protein-coupled receptors (GPCRs) and downstream effectors such as phospholipase C-beta. Its activity couples with proteins like GNA11 another member of the Gq family which often shares overlapping functions and roles within these pathways. The calcium signaling pathway involves GNAQ-induced release of calcium ions contributing to various cellular events.

GNAQ mutations link to uveal melanoma and Sturge-Weber syndrome. Studies show that these mutations activate the MAPK pathway independently promoting uncontrolled cell growth seen in uveal melanoma. GNA11 closely related to GNAQ also frequently undergoes similar mutations in uveal melanoma. In Sturge-Weber syndrome mutation of GNAQ leads to abnormal capillary growth and neurological issues evidencing its pathogenic role in vascular malformations.
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Specifications

Form

Liquid

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General info

Function

Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed : 37991948). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed : 37991948). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed : 37991948). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed : 37991948). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed : 37991948). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation : activates phospholipase C-beta : following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed : 37991948). Required for platelet activation (By similarity). Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (By similarity). Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed : 27852822). Together with GNA11, required for heart development (By similarity).

Sequence similarities

Belongs to the G-alpha family. G(q) subfamily.

Post-translational modifications

Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095). Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane (PubMed:19001095).. (Microbial infection) Deamidated at Gln-209 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.. Histaminylated at Gln-209 residues by TGM2.

Subcellular localisation

Nucleus

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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed : 37991948). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed : 37991948). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed : 37991948). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed : 37991948). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed : 37991948). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation : activates phospholipase C-beta : following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed : 37991948). Required for platelet activation (By similarity). Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (By similarity). Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed : 27852822). Together with GNA11, required for heart development (By similarity).
See full target information GNAQ
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

American journal of physiology. Regulatory, integrative and comparative physiology 318:R38-R48 PubMed31596114

2019

Evidence that hindbrain astrocytes in the rat detect low glucose with a glucose transporter 2-phospholipase C-calcium release mechanism.

Applications

Unspecified application

Species

Unspecified reactive species

Richard C Rogers,Susan J Burke,J Jason Collier,Sue Ritter,Gerlinda E Hermann
View all publications
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