Rabbit Polyclonal GIV phospho S1417 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CCDC88A phospho S1417.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS, 0.88% Sodium chloride
IHC-P | |
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Human | Tested |
Mouse | Predicted |
Species | Dilution info | Notes |
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Species Human | Dilution info 1/50 - 1/100 | Notes Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
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Species Mouse | Dilution info - | Notes - |
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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).
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
Rabbit Polyclonal GIV phospho S1417 antibody. Suitable for IHC-P and reacts with Human samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human CCDC88A phospho S1417.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS, 0.88% Sodium chloride
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.
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.
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.
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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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.
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