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AB111440

Anti-GIV (phospho S1417) antibody

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(2 Publications)

Rabbit Polyclonal GIV phospho S1417 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human CCDC88A phospho S1417.

View Alternative Names

APE, GRDN, KIAA1212, CCDC88A, Girdin, Akt phosphorylation enhancer, Coiled-coil domain-containing protein 88A, G alpha-interacting vesicle-associated protein, Girders of actin filament, Hook-related protein 1, GIV, HkRP1

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-GIV (phospho S1417) antibody (AB111440)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-GIV (phospho S1417) antibody (AB111440)

ab111440, at 1/50 dilution, staining GIV in paraffin-embedded Human breast carcinoma tissue by Immunohistochemistry, in the presence (right panel) or absence (left panel) of immunising peptide.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Synthetic Peptide within Human CCDC88A phospho S1417. The exact immunogen used to generate this antibody is proprietary information.

Q3V6T2

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Alternative Products

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Primary Antibodies

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Complementary Products

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Secondary Antibodies

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Biochemicals

AB144641

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/50 - 1/100", "IHCP-species-notes": "<p></p> Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol." }, "Mouse": { "IHCP-species-checked": "predicted", "IHCP-species-dilution-info": "", "IHCP-species-notes": "" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
ab111440 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.88% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C
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Supplementary information

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

Girdin also known as GIV or Girders of actin filaments plays a significant role in cell signaling. It is a multifunctional adaptor protein with a mass of approximately 220 kDa. GIV is expressed in various tissues including the brain heart and immune cells. It acts as an important player in the reorganization of the actin cytoskeleton which is critical for cellular processes like migration and adhesion.
Biological function summary

GIV is important for modulating signal transduction pathways. It interacts with G-protein coupled receptors (GPCRs) and growth factor receptors facilitating the activation of G-protein signaling. GIV does not typically function alone; it integrates into larger signaling complexes interfacing with other proteins to propagate signals downstream. Through these interactions it influences processes like cell proliferation and survival.

Pathways

GIV significantly impacts the PI3K-Akt and MAPK pathways. It acts as an upstream regulator controlling the activation of signaling cascades that determine cell fate decisions. GIV works closely with proteins such as Akt a central protein in the PI3K pathway and Grb2 linking receptor tyrosine kinases to downstream signaling mechanisms. These interactions highlight GIV’s importance in mediating cellular responses to external stimuli.

GIV’s dysregulation links to cancer and metabolic disorders. In cancer GIV overexpression correlates with enhanced tumor progression and poor patient prognosis. GIV interacts with epidermal growth factor receptor (EGFR) to drive oncogenic signaling promoting tumor survival and growth. In metabolic disorders like diabetes alterations in GIV’s signaling pathways contribute to insulin resistance. Investigations into these interactions highlight the potential for targeting GIV therapeutically using inhibitors like DUB inhibitors and PR-619.
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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

Bifunctional modulator of guanine nucleotide-binding proteins (G proteins) (PubMed : 19211784, PubMed : 27621449). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates guanine nucleotide-binding protein G(i) alpha subunits (PubMed : 19211784, PubMed : 21954290, PubMed : 23509302, PubMed : 25187647). Also acts as a guanine nucleotide dissociation inhibitor for guanine nucleotide-binding protein G(s) subunit alpha GNAS (PubMed : 27621449). Essential for cell migration (PubMed : 16139227, PubMed : 19211784, PubMed : 20462955, PubMed : 21954290). Interacts in complex with G(i) alpha subunits with the EGFR receptor, retaining EGFR at the cell membrane following ligand stimulation and promoting EGFR signaling which triggers cell migration (PubMed : 20462955). Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex which enhances phosphoinositide 3-kinase (PI3K)-dependent phosphorylation and kinase activity of AKT1/PKB (PubMed : 19211784). Phosphorylation of AKT1/PKB induces the phosphorylation of downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA replication and cell proliferation (By similarity). Binds in its tyrosine-phosphorylated form to the phosphatidylinositol 3-kinase (PI3K) regulatory subunit PIK3R1 which enables recruitment of PIK3R1 to the EGFR receptor, enhancing PI3K activity and cell migration (PubMed : 21954290). Plays a role as a key modulator of the AKT-mTOR signaling pathway, controlling the tempo of the process of newborn neuron integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Inhibition of G(s) subunit alpha GNAS leads to reduced cellular levels of cAMP and suppression of cell proliferation (PubMed : 27621449). Essential for the integrity of the actin cytoskeleton (PubMed : 16139227, PubMed : 19211784). Required for formation of actin stress fibers and lamellipodia (PubMed : 15882442). May be involved in membrane sorting in the early endosome (PubMed : 15882442). Plays a role in ciliogenesis and cilium morphology and positioning and this may partly be through regulation of the localization of scaffolding protein CROCC/Rootletin (PubMed : 27623382).
See full target information CCDC88A phospho S1417
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Publications (2)

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

Molecular therapy. Nucleic acids 23:1323-1333 PubMed33717652

2021

SIRT1-induced deacetylation of Akt expedites platelet phagocytosis and delays HEMEC aging.

Applications

Unspecified application

Species

Unspecified reactive species

Yong Lan,Min Dong,Yongjun Li,Yongpeng Diao,Zuoguang Chen,Yangfang Li

International journal of cancer 142:573-583 PubMed28944451

2017

Expression of miRNA-26b-5p and its target TRPS1 is associated with radiation exposure in post-Chernobyl breast cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Christina M Wilke,Julia Hess,Sergiy V Klymenko,Vadim V Chumak,Liubov M Zakhartseva,Elena V Bakhanova,Annette Feuchtinger,Axel K Walch,Martin Selmansberger,Herbert Braselmann,Ludmila Schneider,Adriana Pitea,Julia Steinhilber,Falko Fend,Hans C Bösmüller,Horst Zitzelsberger,Kristian Unger
View all publications
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