Type I ribosome inactivating protein (RIP). Depurinates RNA in ribosomes, thus inhibiting protein synthesis in eukaryotic cells, which results in cell death. Widely used to construct immunotoxins composed of cell-targeted antibodies. As a type I RIP it lacks the lectin subunit and is practically non-toxic to intact cells. Inhibits cell-free protein synthesis in reticulocyte assay with globin messenger (IC50=4.5ng/ml).
Product Details
MW: | ~30kDa |
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Source: | Isolated from Gelonium multiflorum. |
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CAS: | 75037-46-6 |
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UniProt ID: | P33186 |
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Concentration: | ~2mg/ml |
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Formulation: | Liquid. In 5mM phosphate buffer, pH 6.5, containing 5mM EDTA and 120mM sodium chloride. |
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Purity: | ≥95% |
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Shipping: | Dry Ice |
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Long Term Storage: | -80°C |
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Regulatory Status: | RUO - Research Use Only |
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Figure: SDS-PAGE (12% polyacrylamidgel)Lane 1: Gelonin,5µgLane 2: Proteinmarker (200-6,5 kDa)
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Product Literature References
Sequentially Self-Assembled Nanoreactor Comprising Tannic Acid and Phenylboronic Acid-Conjugated Polymers Inducing Tumor-Selective Enzymatic Activity: Y. Honda, et al.; ACS Appl. Mater. Interfaces
13, 54850 (2021),
Abstract;
Immunotoxin Against a Donor MHC Class II Molecule Induces Indefinite Survival of Murine Kidney Allografts: K. Brown, et al.; Am. J. Transplant.
16, 1129 (2016),
Application(s): Cell death,
Abstract;
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Intracellular re-localisation by photochemical internalisation enhances the cytotoxic effect of gelonin--quantitative studies in normal rat liver: J. Woodhams, et al.; J. Contr. Rel.
142, 347 (2010),
Abstract;
Multimodality molecular imaging of glioblastoma growth inhibition with vasculature-targeting fusion toxin VEGF121/rGel: A.R. Hsu, et al.; J. Nucl. Med.
48, 445 (2007),
Abstract;
Novel immunotoxin: a fusion protein consisting of gelonin and an acetylcholine receptor fragment as a potential immunotherapeutic agent for the treatment of Myasthenia gravis: M. Hossann, et al.; Protein Expr. Purif.
46, 73 (2006),
Abstract;
On the contentious sequence and glycosylation motif of the ribosome inactivating plant protein gelonin: T. Daubenfeld, et al.; BBRC
333, 984 (2005),
Abstract;
Intein-mediated fusion expression, high efficient refolding, and one-step purification of gelonin toxin: C. Guo, et al.; Protein Expr. Purif.
37, 361 (2004),
Abstract;
Gelonin is an unusual DNA glycosylase that removes adenine from single-stranded DNA, normal base pairs and mismatches: E. Nicolas, et al.; J. Biol. Chem.
275, 31399 (2000),
Abstract;
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Comparative cytotoxicity and pharmacokinetics of antimelanoma immunotoxins containing either natural or recombinant gelonin: M.G. Rosenblum, et al.; Cancer Chemother. Pharmacol.
44, 343 (1999),
Abstract;
Identity elements in bovine tRNA(Trp) required for the specific stimulation of gelonin, a plant ribosome-inactivating protein: M. Brigotti, et al.; RNA
5, 1357 (1999),
Abstract;
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Purification and characterisation of gelonin from seeds of Gelonium multiflorum: V. Singh, et al.; Indian J. Biochem. Biophys.
36, 258 (1999),
Abstract;
A new class of DNA glycosylase/apurinic/apyrimidinic lyases that act on specific adenines in single-stranded DNA: E. Nicolas, et al.; J. Biol. Chem.
273, 17216 (1998),
Abstract;
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Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin: E. Nicolas, et al.; FEBS Lett.
406, 162 (1997),
Abstract;
Amino acid sequence analysis, gene construction, cloning, and expression of gelonin, a toxin derived from Gelonium multiflorum: M.G. Rosenblum, et al.; J. Interferon Cytokine Res.
15, 547 (1995),
Abstract;
Differential sensitivity of CD30+ neoplastic cells to gelonin delivered by anti-CD30/anti-gelonin bispecific antibodies: S. Sforzini, et al.; Br. J. Haematol.
90, 572 (1995),
Abstract;
Gelonin analogs with engineered cysteine residues form antibody immunoconjugates with unique properties: M. Better, et al.; J. Biol. Chem.
269, 9644 (1994),
Abstract;
Antigen-specific therapy of experimental myasthenia gravis with acetylcholine receptor-gelonin conjugates in vivo: I.L. Urbatsch, et al.; Eur. J. Immunol.
23, 776 (1993),
Abstract;
Cloning and expression of a gene encoding gelonin, a ribosome-inactivating protein from Gelonium multiflorum: P.A. Nolan, et al.; Gene
134, 223 (1993),
Abstract;
Structural characterization of gelonin: evidence for separate antigenic and cytotoxic domains: M.R. Sairam, et al.; Biochem. Mol. Biol. Int.
31, 575 (1993),
Abstract;
Toxin-targeted design for anticancer therapy. II: Preparation and biological comparison of different chemically linked gelonin-antibody conjugates: L. Delprino, et al.; J. Pharm. Sci.
82, 699 (1993),
Abstract;
Monoclonal antibodies to gelonin: production and characterization: J. Zimmermann & W.E. Trommer; Hybridoma
10, 65 (1991),
Abstract;
Requirements for the inactivation of ribosomes by gelonin: S. Sperti, et al.; Biochem. J.
277, 281 (1991),
Abstract;
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The antileukemic efficacy of an immunotoxin composed of a monoclonal anti-Thy-1 antibody disulfide linked to the ribosome-inactivating protein gelonin: C.F. Scott, Jr., et al.; Cancer Immunol. Immunother.
25, 31 (1987),
Abstract;
Gelonin, a new inhibitor of protein synthesis, nontoxic to intact cells. Isolation, characterization, and preparation of cytotoxic complexes with concanavalin: A: F. Stirpe, et al.; J. Biol. Chem.
255, 6947 (1980),
Abstract;
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