Recombinant Human GBP1 protein
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(1 Publication)
Recombinant Human GBP1 protein is a Human Full Length protein, in the 1 to 592 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
Guanylate-binding protein 1, GTP-binding protein 1, Guanine nucleotide-binding protein 1, Interferon-induced guanylate-binding protein 1, GBP-1, HuGBP-1, hGBP1, GBP1
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human GBP1 protein (AB114960)
12.5% SDS-PAGE showing ab114960 at approximately 91.23kDa.
Stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The GBP1 protein supports cellular defense mechanisms against pathogens such as viruses and bacteria. GBP1 participates in the hydrolysis of GTP to GMP an action that influences its anti-pathogenic effects. It is a member of the interferon-inducible large GTPase family and can form oligomeric complexes enhancing its antiviral and antimicrobial activity. It interacts with various proteins linked to innate immunity and contributes to modulating the immune response.
Pathways
GBP1 is involved in pathways linked to interferon signaling and innate immunity. The protein plays a significant role in the JAK-STAT signaling pathway where it exerts its antiviral effects. GBP1 interacts closely with other proteins such as STAT1 and is responsive to interferon signals influencing gene expression and immune responses. Its activity in these pathways is critical for mounting an effective defense against infections.
Specifications
Form
Liquid
General info
Function
Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed : 16511497, PubMed : 22106366, PubMed : 29144452, PubMed : 31268602, PubMed : 32510692, PubMed : 32581219, PubMed : 37797010, PubMed : 7512561). Hydrolyzes GTP to GMP in two consecutive cleavage reactions : GTP is first hydrolyzed to GDP and then to GMP in a processive manner (PubMed : 16511497, PubMed : 32510692, PubMed : 7512561). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and promotes both inflammasome assembly and autophagy (PubMed : 29144452, PubMed : 31268602). Acts as a positive regulator of inflammasome assembly by facilitating the detection of inflammasome ligands from pathogens (PubMed : 31268602, PubMed : 32510692, PubMed : 32581219). Involved in the lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (By similarity). Following pathogen release in the cytosol, forms a protein coat in a GTPase-dependent manner that encapsulates pathogens and promotes the detection of ligands by pattern recognition receptors (PubMed : 32510692, PubMed : 32581219). Plays a key role in inflammasome assembly in response to infection by Gram-negative bacteria : following pathogen release in the cytosol, forms a protein coat that encapsulates Gram-negative bacteria and directly binds to lipopolysaccharide (LPS), disrupting the O-antigen barrier and unmasking lipid A that is that detected by the non-canonical inflammasome effector CASP4/CASP11 (PubMed : 32510692, PubMed : 32581219). Also promotes recruitment of proteins that mediate bacterial cytolysis, leading to release double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (PubMed : 31268602). Involved in autophagy 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 (By similarity). 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).
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
Post-translational modifications
Isoprenylation is required for proper subcellular location.. Phosphorylated at Ser-156 by PIM1 in absence of infection, inhibits GBP1: phosphorylation promotes interaction with 14-3-3 protein sigma (SFN), leading to GBP1 retention in the cytosol (PubMed:37797010). Dephosphorylated in response to infection, liberating GBP1 (PubMed:37797010).. (Microbial infection) Ubiquitinated by S.flexneri IpaH9.8, leading to its degradation by the proteasome, thereby preventing its ability to promote host defense against bacterial infection.
Target data
Publications (1)
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Science (New York, N.Y.) 382:eadg2253 PubMed37797010
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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