Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
GBP1 Antibody (N-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P32455 |
|---|---|
| Clone Names | 100318065 |
| Gene ID | 2633 |
|---|---|
| Other Names | Interferon-induced guanylate-binding protein 1, GTP-binding protein 1, GBP-1, HuGBP-1, Guanine nucleotide-binding protein 1, GBP1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | GBP1 {ECO:0000303|PubMed:7512561, ECO:0000312|HGNC:HGNC:4182} |
|---|---|
| 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:7512561, PubMed:37797010, PubMed:32510692, PubMed:32581219). 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). |
| Cellular Location | Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytosol. Secreted. Note=Localizes to pathogen-containing vacuoles or to the cell surface of bacteria that escaped vacuoles (PubMed:29144452, PubMed:31268602, PubMed:32510692, PubMed:32581219) 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) Sequestered in the cytosol following phosphorylation by PIM1 and subsequent interaction with 14-3-3 protein sigma (SFN) (PubMed:37797010). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
Guanylate binding protein expression is induced byinterferon. Guanylate binding proteins are characterized by theirability to specifically bind guanine nucleotides (GMP, GDP, andGTP) and are distinguished from the GTP-binding proteins by thepresence 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)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
