Gelonin



ALX-350-150-M001	1 mg	190.00 USD

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=2.7ng/ml).

Product Specification

Concentration:	2.1mg/ml

MW:	~30kDa

Purity:	≥95%

Formulation:	Liquid. In 5mM phosphate buffer, pH 6.5, containing 5mM EDTA and 120mM sodium chloride.

CAS:	75037-46-6

Source/Host:	Isolated from Gelonium multiflorum.

Shipping:	SHIPPED ON DRY ICE

Long Term Storage:	-80°C

Hazard:	HARMFUL.

Product Literature References

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; Full Text

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;

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; Full Text

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;

Gelonin analogs with engineered cysteine residues form antibody immunoconjugates with unique properties: M. Better, et al.; J. Biol. Chem. 269, 9644 (1994), 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;

Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin: E. Nicolas, et al.; FEBS Lett. 406, 162 (1997), 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; Full Text

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; Full Text

Purification and characterisation of gelonin from seeds of Gelonium multiflorum: V. Singh, et al.; Indian J. Biochem. Biophys. 36, 258 (1999), 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; Full Text

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;

On the contentious sequence and glycosylation motif of the ribosome inactivating plant protein gelonin: T. Daubenfeld, et al.; BBRC 333, 984 (2005), 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;

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;