Anti-GBP1 / Guanylate binding protein 1, clone GBP1/7617

1 mg/ml in 1X PBS, BSA free, sodium azide free. GBP1 (guanylate binding protein 1) is a 592 amino acid protein member of the GTPase protein family and is able to bind specifically to guanine nucleotides such as GMP, GDP and GTP. GMP is hydrolyzed to GTP in two consecutive cleavage steps, both of which are carried out by GBP1. Localized to the cytoplasm, GBP1 is expressed in endothelial cells of the vascular system and is induced by IFN-g during macrophage induction. GBP1 is thought to regulate the expression of MMP-1, which mediates the proliferation and invasiveness of endothelial cells. GBP1 plays a key role in regulating inflammatory cytokines and provides protection against vesicular stomatitis and encephalomyocarditis viruses. GBP1 expression is highly induced in the vessels of skin diseases such as psoriasis and Kaposi s sarcoma, making it a novel cellular activation marker that characterizes inflammatory cytokines of endothelial cells. Protein function: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:22106366, PubMed:29144452, PubMed:16511497, PubMed:31268602). Hydrolyzes GTP to GMP in two consecutive cleavage reactions: GTP is first hydrolyzed to GDP and then to GMP in a processive manner (PubMed:7512561, PubMed:16511497). Following infection, recruited to the pathogen-containing vacuoles or vacuole- escaped bacteria and promotes both autophagy and inflammasome assembly (PubMed:29144452, PubMed:31268602). Promotes host defense against bacterial infections by regulating bacteriolytic peptide generation via its interaction with ubiquitin-binding protein SQSTM1, which delivers monoubiquitinated proteins to autolysosomes for the generation of bacteriolytic peptides. Also acts as a positive regulator of inflammasome assembly by promoting the release of inflammasome ligands from bacteria (PubMed:31268602). Acts by promoting lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol. Following pathogen release in the cytosol, promotes recruitment of proteins that mediate bacterial cytolysis: this liberates ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed:31268602). Confers protection to several pathogens, including the bacterial pathogens L.monocytogenes and M.bovis BCG as well as the protozoan pathogen T.gondii (PubMed:31268602). Exhibits antiviral activity against influenza virus (PubMed:22106366). [The UniProt Consortium]