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AB113585

Recombinant Human GNAI1 protein

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(1 Publication)

Recombinant Human GNAI1 protein is a Human Full Length protein, in the 1 to 354 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

Guanine nucleotide-binding protein G(i) subunit alpha-1, Adenylate cyclase-inhibiting G alpha protein, GNAI1

1 Images
SDS-PAGE - Recombinant Human GNAI1 protein (AB113585)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human GNAI1 protein (AB113585)

3ug by SDS-PAGE under reducing conditions and visualized by coomassie blue stain.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P63096

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.32% Tris HCl

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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as G protein alpha inhibitor 1, G Protein alpha Inhibitor 1+2
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSMGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF","proteinLength":"Full Length","predictedMolecularWeight":"42.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":354,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P63096","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°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.

The protein GNAI1 also known as G protein subunit alpha i1 is part of the G-protein family that plays an important role in signal transduction. GNAI1 has a molecular mass of approximately 40 kDa. It is mainly expressed in neuronal tissues where it interacts with receptors to regulate intracellular signaling pathways. This protein operates by inhibiting adenylate cyclase activity which reduces the production of cyclic AMP (cAMP) in response to extracellular signals.
Biological function summary

GNAI1 acts by interfering with signal transmission across membranes. It is part of the heterotrimeric G-protein complex which is essential for many signaling processes. This complex responds to activation by G-protein-coupled receptors (GPCRs) and modulates various downstream effectors essentially affecting numerous physiological processes like neurotransmission and hormone signaling.

Pathways

GNAI1 plays a significant role in the cyclic AMP (cAMP) signaling pathway and the neuroactive ligand-receptor interaction pathway. In the cAMP pathway GNAI1 associates with receptors like dopamine and serotonin receptors helping to regulate neuronal response and neurotransmitter release. This activity involves interactions with related proteins such as GNB1 and GNG2 which form the beta and gamma subunits of the heterotrimeric G-protein complex.

GNAI1 relates to neuropathic conditions such as epilepsy and depression. Alterations in GNAI1 function can disrupt normal signaling contributing to these disorders. The protein interacts with other proteins in the signaling cascade such as RGS proteins which can affect its function in disease states. Researchers continue to explore how modifications or mutations in GNAI1 might offer potential therapeutic targets for these and similar disorders.
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Specifications

Form

Liquid

Additional notes

ab113585 was purified using conventional chromatography.

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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 : 18434541, PubMed : 33762731, PubMed : 34239069, PubMed : 35610220, PubMed : 37935376, PubMed : 37935377, PubMed : 37963465, PubMed : 38552625, PubMed : 8774883). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed : 18434541, PubMed : 8774883). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed : 18434541, PubMed : 8774883). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed : 18434541, PubMed : 8774883). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed : 18434541, PubMed : 8774883). Signaling is mediated via effector proteins, such as adenylate cyclase : inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels (PubMed : 8119955). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed : 17635935). Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed : 22327364).

Sequence similarities

Belongs to the G-alpha family. G(i/o/t/z) subfamily.

Post-translational modifications

Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.. Palmitoylation at Cys-3 varies with membrane lipid composition.. (Microbial infection) Deamidated at Gln-204 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.

Subcellular localisation

Nucleus

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Product protocols

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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 : 18434541, PubMed : 33762731, PubMed : 34239069, PubMed : 35610220, PubMed : 37935376, PubMed : 37935377, PubMed : 37963465, PubMed : 38552625, PubMed : 8774883). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed : 18434541, PubMed : 8774883). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed : 18434541, PubMed : 8774883). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed : 18434541, PubMed : 8774883). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed : 18434541, PubMed : 8774883). Signaling is mediated via effector proteins, such as adenylate cyclase : inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels (PubMed : 8119955). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed : 17635935). Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed : 22327364).
See full target information GNAI1
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Publications (1)

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

Cell biology international 44:1142-1155 PubMed31965656

2020

Role of PKCζ-NADPH oxidase signaling axis in PKCα-mediated Giα2 phosphorylation for inhibition of adenylate cyclase activity by angiotensin II in pulmonary artery smooth muscle cells.

Applications

Unspecified application

Species

Unspecified reactive species

Animesh Chowdhury,Jaganmay Sarkar,Pijush Kanti Pramanik,Tapati Chakraborti,Sajal Chakraborti
View all publications
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