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Human GBP2 Protein expressed in Human Cells - ABIN2006014
Wistow, Bernstein, Wyatt, Fariss, Behal, Touchman, Bouffard, Smith, Peterson: Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants. in Molecular vision 2002
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Gtpbp2 is required for BMP signaling and mesoderm patterning in Xenopus embryos.
Low GBP2 expression is associated with metastasis in breast cancer.
GBP1 (show GBP1 Proteins)/2 are critical effectors of antichlamydial interferon (IFN)gamma (show IFNA Proteins)-mediated pathogen clearance via rerouting of bacterial inclusions in macrophages for lysosomal degradation.
Downregulation of MIR (show MLXIP Proteins)-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 (show RACGAP1 Proteins) activity for GMP (show NT5C2 Proteins) 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 (show PNN Proteins) Gbp2p and phosphorylates all three serines present in a contiguous RS dipeptide stretch
GBP-2 is regulated by p53 (show TP53 Proteins) and may have a role in esophageal squamous cell carcinomas
GBP1 (show GBP1 Proteins) 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 (show AIM2 Proteins) during infection with F. novicida.
This study begins to define the properties of mGBP-2 responsible for inhibiting cell spreading.
these results not only define GTPBP2 as a ribosome rescue factor but also unmask the disease potential of mutations in nuclear-encoded tRNA genes.
Murine guanylate binding protein 2 (mGBP2) controls Toxoplasma gondii replication.
the inducible multimerization of mGBP2 is dependent on a functional GTPase (show RACGAP1 Proteins) domain.
IRGM (show IRGM Proteins) 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 (show TNF Proteins) activation of endogenous Rac1 and constitutively activate Rac (show AKT1 Proteins) can restore NF-kappaB (show NFKB1 Proteins) transcription in the presence of mGBP-2. This is a novel mechanism by which IFNs can inhibit the cytokine induction of MMP-9 (show MMP9 Proteins) expression.
Both IFN-gamma (show IFNG Proteins) and mGBP-2 also inhibit cell spreading initiated by platelet-derived growth factor treatment, which is also accompanied by inhibition of Rac (show AKT1 Proteins) activation by mGBP-2.
inhibits replication of both vesicular stomatitis virus (VSV) and encephalomyocarditis virus (EMCV); a wild type GTP binding (show RND2 Proteins) motif was not required for VSV inhibition but was required for inhibition of EMCV
cDNA sequences were cloned and the genomic structure of porcine GBP1 (show GBP1 Proteins) (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
, GTP-binding-like protein 2
, guanine nucleotide-binding protein 2
, guanylate nucleotide binding protein 2
, interferon-induced guanylate-binding protein 2
, isoprenylated 67 kDa protein