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AB114960

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

1 Images
SDS-PAGE - Recombinant Human GBP1 protein (AB114960)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human GBP1 protein (AB114960)

12.5% SDS-PAGE showing ab114960 at approximately 91.23kDa.
Stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

Tag free

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

P32455

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Recombinant protein.</p>" } } }

Sequence info

[{"sequence":"MASEIHMTGPMCLIENTNGRLMANPEALKILSAITQPMVVVAIVGLYRTGKSYLMNKLAGKKKGFSLGSTVQSHTKGIWMWCVPHPKKPGHILVLLDTEGLGDVEKGDNQNDSWIFALAVLLSSTFVYNSIGTINQQAMDQLYYVTELTHRIRSKSSPDENENEVEDSADFVSFFPDFVWTLRDFSLDLEADGQPLTPDEYLTYSLKLKKGTSQKDETFNLPRLCIRKFFPKKKCFVFDRPVHRRKLAQLEKLQDEELDPEFVQQVADFCSYIFSNSKTKTLSGGIQVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVQKAIAHYEQQMGQKVQLPTESLQELLDLHRDSEREAIEVFIRSSFKDVDHLFQKELAAQLEKKRDDFCKQNQEASSDRCSGLLQVIFSPLEEEVKAGIYSKPGGYRLFVQKLQDLKKKYYEEPRKGIQAEEILQTYLKSKESMTDAILQTDQTLTEKEKEIEVERVKAESAQASAKMLQEMQRKNEQMMEQKERSYQEHLKQLTEKMENDRVQLLKEQERTLALKLQEQEQLLKEGFQKESRIMKNEIQDLQTKMRRRKACTIS","proteinLength":"Full Length","predictedMolecularWeight":"91.23 kDa","actualMolecularWeight":null,"aminoAcidEnd":592,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P32455","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The target known commonly as GBP1 or guanylate-binding protein 1 plays a mechanical role as a large GTPase with a molecular mass of approximately 67 kDa. This protein is expressed in various tissues most notably in interferon-gamma-induced human cells. GBP1 localizes mainly in the cytoplasm and associates with cellular membranes. Alternate designations for the GBP1 protein include GBP 1. Its role as a GTPase involves hydrolyzing GTP which is critical for its cellular functions.
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.

GBP1 has been associated with inflammatory diseases and cancer. The protein's expression levels often increase in response to inflammatory signals implicating it in the pathogenesis of diseases like Crohn's disease. Moreover GBP1 has a connection with cancer-related mechanisms where it might affect tumor cell proliferation. In these contexts proteins such as STAT1 and other interferon-responsive proteins relate closely to the function and regulatory mechanisms of GBP1.

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.

Product protocols

Target data

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).
See full target information GBP1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Science (New York, N.Y.) 382:eadg2253 PubMed37797010

2023

PIM1 controls GBP1 activity to limit self-damage and to guard against pathogen infection.

Applications

Unspecified application

Species

Unspecified reactive species

Daniel Fisch,Moritz M Pfleiderer,Eleni Anastasakou,Gillian M Mackie,Fabian Wendt,Xiangyang Liu,Barbara Clough,Samuel Lara-Reyna,Vesela Encheva,Ambrosius P Snijders,Hironori Bando,Masahiro Yamamoto,Andrew D Beggs,Jason Mercer,Avinash R Shenoy,Bernd Wollscheid,Kendle M Maslowski,Wojtek P Galej,Eva-Maria Frickel
View all publications

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