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Study presents the first demonstration that GBP2 inhibits mitochondrial fission and cell metastasis in breast cancer cells both in vitro and in vivo.
Low GBP2 expression is associated with metastasis in breast cancer.
GBP1/2 are critical effectors of antichlamydial interferon (IFN)gamma-mediated pathogen clearance via rerouting of bacterial inclusions in macrophages for lysosomal degradation.
Downregulation of MIR-433 is associated with myeloproliferative neoplasms.
The in vivo localization of GBP-2 at cellular membranes is regulated by isoprenylation and dimerization.
hGBP-1, hGBP-2 showed dimerization-related GTPase activity for GMP formation.
Guanylate-binding protein 2 mRNA in peripheral blood leukocytes may have a role in acute cellular rejection after liver transplantation
Sky1p utilizes the same docking groove to bind yeast SR-like protein Gbp2p and phosphorylates all three serines present in a contiguous RS dipeptide stretch
GBP-2 is regulated by p53 and may have a role in esophageal squamous cell carcinomas
GBP2 can effectively regulate beta-glucan-induced maturation of DCs, thus suppressing the proliferation of T cells.
This study demonstrated that Gbeta2 is important for neuronal migration, especially in the multipolar-bipolar transition.
GBP1 GBP2 enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages.
this study identified guanylate-binding proteins GBP2 and GBP5 as key activators of AIM2 during infection with F. novicida.
This study begins to define the properties of mGBP-2 responsible for inhibiting cell spreading.
Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replication.
the inducible multimerization of mGBP2 is dependent on a functional GTPase domain.
IRGM proteins indirectly modulate the localization of GBP2 through a distinct mechanism from that through which they regulate IRG protein localization
mGBP-2 inhibits TNF-alpha activation of endogenous Rac1 and constitutively activate Rac can restore NF-kappaB transcription in the presence of mGBP-2. This is a novel mechanism by which IFNs can inhibit the cytokine induction of MMP-9 expression.
Both IFN-gamma and mGBP-2 also inhibit cell spreading initiated by platelet-derived growth factor treatment, which is also accompanied by inhibition of Rac activation by mGBP-2.
inhibits replication of both vesicular stomatitis virus (VSV) and encephalomyocarditis virus (EMCV); a wild type GTP binding motif was not required for VSV inhibition but was required for inhibition of EMCV
mGBP-2, confers resistance to paclitaxel-induced cytotoxicity without inhibiting multinucleation.
The data support the assumption that the main role of STAT1 in activating gbp2 transcription is to provide transcriptionally competent chromatin, whereas the function of IRF1 may lie in directly contacting RNA polymerase II complexes.
cDNA sequences were cloned and the genomic structure of porcine GBP1 (poGBP1) and GBP2 (poGBP2), was analyzed.
Interferons are cytokines that have antiviral effects and inhibit tumor cell proliferation. They induce a large number of genes in their target cells, including those coding for the guanylate-binding proteins (GBPs). GBPs are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP). The protein encoded by this gene is a GTPase that converts GTP to GDP and GMP.
GTP-binding protein 2
, guanine nucleotide-binding protein 2
, interferon-induced guanylate-binding protein 2
, guanylate nucleotide binding protein 2
, isoprenylated 67 kDa protein