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Human Monoclonal GBP1 Primary Antibody for IHC (p), ELISA - ABIN515966
Ascierto, Kmieciak, Idowu, Manjili, Zhao, Grimes, Dumur, Wang, Ramakrishnan, Wang, Bear, Marincola, Manjili: A signature of immune function genes associated with recurrence-free survival in breast cancer patients. in Breast cancer research and treatment 2012
this demonstrated that the alpha9-helix is the proliferation inhibitory domain of GBP-1, which acts independent of the GTPase activity through the inhibition of the Hippo transcription factor TEAD in mediating the anti-proliferative cell response to IFN-gamma.
we identified that the LG domains of hGBP-1 and hGBP-5 build an interaction site within the hetero dimer. Our in vitro study provides mechanistic insights into the homomeric and heteromeric interactions of hGBP-1 and hGBP-5 and present useful strategies to characterise the hGBP network further.
we have found GBP1 was downregulated during osteogenic differentiation of hBM-MSCs. While knockdown of GBP1 promoted osteogenesis, overexpression of GBP1 suppressed osteogenesis of hBM-MSCs.
Here, we show that the human protein GBP1 acts as a cytosolic "glue trap," capturing cytosolic Gram-negative bacteria through a unique protein motif and preventing disseminated infections in cell culture models. To escape from this GBP1-mediated host defense, Shigella employs a virulence factor that prevents or dislodges the association of GBP1 with cytosolic bacteria.
Results show that GBP1 is overexpressed in triple-negative breast cancer (TNBC), under the control of EGFR and selectively affects the growth of TNBC cell lines.
hGBP1F acts as a nucleotide-controlled molecular switch by modulating the accessibility of its farnesyl moiety, which does not require any supportive proteins
These findings confirm the involvement of caspase-1 in non-classical secretion mechanisms and open novel perspectives for the extracellular function of secreted GBP-1.
Results suggest that guanylate-binding protein 1 (GBP1) plays a pivotal role in anti-T. gondii protection of mesenchymal stromal cells (hMSCs) and may shed new light on clarifying the mechanism of host defense properties of hMSCs.
Shigella flexneri infection induces rapid proteasomal degradation of human guanylate binding protein-1 (hGBP1); the mode of IpaH9.8 action highlights the functional importance of GBPs in antibacterial defenses
Previously reported tetrameric and dimeric species of hGBP-1 and hGBP-5 were unmasked as dimers and monomers, respectively, with their shapes depending on both the bound nucleotide and the ionic strength of the solution.
Taken together, these results provide a new understanding of the antiviral mechanism of human GBP1, which possesses potent anti-Kaposi's sarcoma-associated herpesvirus activity, and suggest the critical role of viral RTA in the evasion of the innate immune response during primary infection by Kaposi's sarcoma-associated herpesvirus.
A novel role for hGBP1 in cell-autonomous immunity that is independent of pathogen-containing vacuole translocation.
Elevated hGBP-1 RNA in ovarian tumors correlates with shorter recurrence-free survival. hGBP-1 does not confer paclitaxel resistance on MCF-7 and TMX2-28 breast cancer cells.
In insulitic islets from living patients with recent-onset T1D, most of the overexpressed ISGs, including GBP1, TLR3, OAS1, EIF2AK2, HLA-E, IFI6, and STAT1, showed higher expression in the islet core compared with the peri-islet area containing the surrounding immune cells
the study not only highlights the importance of hGBP1 tetramer in stimulated GMP formation, but also demonstrates its role in the antiviral activity against hepatitis C virus.
GBP1 expression is elevated in human Glioblastoma multiforme tumors and positively correlates with EGFRvIII status in Glioblastoma multiforme specimens, and its expression is inversely correlated with the survival rate of Glioblastoma multiforme patients. Taken together, these results reveal that GBP1 may serve as a potential therapeutic target for Glioblastoma multiforme with EGFRvIII mutation.
GBP1 promotes lymph node metastasis and has a positive correlation with EGFR expression in esophageal squamous cell carcinoma.
Molecular dynamics studies showed that only GTP decreases the formation of the GBP1:PIM1 complex through an allosteric mechanism, outlining the rational for the identification of new compounds potentially able to revert resistance to paclitaxel.
GBP1 overexpression is necessary for the radioresistant phenotype in clinically relevant radioresistant cells
data show that dimer formation of hGBP1 involves multiple spatially distant regions of the protein, namely, the N-terminal LG domain and the C-terminal helices alpha13.
GBP1 is associated with resistance against porcine reproductive and respiratory syndrome infection and efficient T cell activation in pigs.
Allele A in GBP1, the unfavourable allele, is associated with higher PRRSV viremia levels and lower weight gain following infection
cDNA sequences were cloned and the genomic structure of porcine GBP1 (poGBP1) and GBP2 (poGBP2), was analyzed.
Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.
, GTP-binding protein 1
, guanine nucleotide-binding protein 1
, guanylate binding protein 1, interferon-inducible, 67kDa
, interferon-induced guanylate-binding protein 1
, guanylate binding protein 1, interferon-inducible