GBP1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, E |
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Primary Accession | P32455 |
Other Accession | NP_002044.2 |
Reactivity | Human |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 67931 Da |
Antigen Region | 141-170 aa |
Gene ID | 2633 |
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Other Names | Interferon-induced guanylate-binding protein 1, GTP-binding protein 1, GBP-1, HuGBP-1, Guanine nucleotide-binding protein 1, GBP1 |
Target/Specificity | This GBP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 141-170 amino acids from the N-terminal region of human GBP1. |
Dilution | WB~~1:1000 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | GBP1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | GBP1 |
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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 (By similarity). 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 (By similarity). 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). |
Cellular Location | Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm Secreted. Note=Localizes to pathogen- containing vacuoles or to the cell surface of bacteria that escaped vacuoles (PubMed:29144452, PubMed:31268602). Secreted from endothelial cells in the cerebrospinal fluid, upon bacterial challenge and independently of IFNG induction (PubMed:16936281). Golgi membrane localization requires isoprenylation and the presence of another IFNG- induced factor (PubMed:15937107). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to specifically bind guanine nucleotides (GMP, GDP, and GTP) and are distinguished from the GTP-binding proteins by the presence of 2 binding motifs rather than 3.
References
Vopel, T., et al. J. Mol. Biol. 400(1):63-70(2010)
Mirpuri, J., et al. J. Immunol. 184(12):7186-7195(2010)
Lipnik, K., et al. Mol. Med. 16 (5-6), 177-187 (2010) :
Davila, S., et al. Genes Immun. 11(3):232-238(2010)
O'Doherty, C., et al. Pharmacogenomics 10(7):1177-1186(2009)
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