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α-Gal Epitope (Galα1-3Galβ1-4GlcNAc-R) monoclonal antibody (M86)

 
ALX-801-090-1 1 Vial 410.00 USD
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Widely described antibody against α-galactose residues with broad cross-reactivity among different species. Useful for measuring the α-Gal epitope expression on cells, glycolipids and glycoproteins, characterization of hyperacute rejection (HAR) in organ and tissue transplantations and monitoring xenotransplantation experiments. The IgM isotype mimicks in vivo reactions and can be used for cytotoxicity assays for α-Gal specific pathways (addition or presence of complement necessary). Ideal as a high-throughput screening tool for inhibitors of antibody induced cytotoxicity.
Organ transplantation from pig to human result in HAR. Humans naturally produce large quantities of anti-α-Gal antibodies, which represent 1-3% of all circulating immunoglobulins and are produced by about 1% of all B cells. When pig organs or tissues are transplanted into the human body, the IgM isotype of anti-Gal binds to α-Gal epitopes, which causes activation of the complement cascade, resulting in cell lysis. This rapid activation of complement by anti-Gal IgM is an immunological barrier that poses the greatest risk of initiating HAR. The monoclonal antibody M86 to Galα1-3Gal epitopes developed by U. Galili, et al. is an essential tool in the study of human xenotransplantation and related research.

Product Specification

Alternative Name:α-Galactose 1,3
 
Clone:M86
 
Host:Mouse
 
Isotype:IgM
 
Immunogen:Rabbit red blood cell membrane.
 
Source:Hybridoma tissue culture.
 
Species reactivity:Mouse, Rat
Porcine
 
Specificity:Recognizes synthetic and naturally produced mouse, rat and pig Galα1-3Gal epitopes on glycoproteins and glycolipids.
 
Crossreactivity:Does not cross-react with β-Gal glycoproteins or BSA.
 
Applications:ELISA, Flow Cytometry, IHC (PS), WB, FUNC
 
Recommended Dilutions/Conditions:Note: Do not use non-fat milk for blocking! Many blocking agents from non-human mammal sources will cross-react with the antibody.
Appropriate antibody dilution may vary from lot to lot. An initial dilution of 1:5 is recommended.
Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application.
 
Application Notes:Functional Application: can be used for cytotoxicity assays for α-Gal specific pathways
 
Quantity:4 mL per vial
 
Formulation:Liquid. Tissue culture supernatant.
 
Use/Stability:Stable for at least 3 years when stored at -20°C.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-20°C
 

Product Literature References

Feasibility of pig and human-derived aortic valve interstitial cells seeding on fixative-free decellularized animal pericardium: R. Santoro, et al.; J. Biomed. Mater. Res. B Appl. Biomater. 104, 345 (2016), Abstract;
In vivo xenogeneic scaffold fate is determined by residual antigenicity and extracellular matrix preservation: M.L. Wong, et al.; Biomaterials 92, 1 (2016), Application(s): Western blot, Abstract;
Immunoproteomics of processed beef proteins reveal novel galactose‐α‐1, 3‐galactose‐containing allergens: D. Apostolovic, et al.; Allergy 69, 1308 (2014), Abstract;
Laminin γ‐1 and collagen α‐1 (VI) chain are galactose‐α‐1, 3‐galactose–bound allergens in beef: H. Takahashi, et al.; Allergy 69, 199 (2014), Abstract;
Novel human renal proximal tubular cell line for the production of complex proteins: L. Fliedl, et al.; J. Biotechnol. 176, 29 (2014), Application(s): Flow cytometry, Abstract;
Possible role of a cell surface carbohydrate in evolution of resistance to viral infections in old world primates: I.A. Rodriguez, et al.; J. Virol. 87, 8317 (2013), Abstract;
Stepwise solubilization-based antigen removal for xenogeneic scaffold generation in tissue engineering: M.L. Wong, et al.; Acta Biomater. 9, 6492 (2013), Application(s): IHC on bovine tissue, Abstract;
Anaphylaxis to pork kidney is related to IgE antibodies specific for galactose-alpha-1,3-galactose: M. Morisset, et al.; Allergy 67, 699 (2012), Abstract;
Complete absence of the αGal xenoantigen and isoglobotrihexosylceramide in α1,3galactosyltransferase knock-out pigs: Y.G.L. Puga, et al.; Xenotransplantation 19, 196 (2012), Application(s): Expression of Galα1,3Gal in pig aortic endothelial cells by flow and and in permeabilized by microscopy, Abstract; Full Text
Generation of bioengineered corneas with decellularized xenografts and human keratocytes: M. Gonzalez-Andrades, et al.; Invest. Ophthalmol. Vis. Sci. 52, 215 (2011), Abstract; Full Text
Brief report: a new profile of terminal N-acetyllactosamines glycans on pig red blood cells and different expression of alpha-galactose on Sika deer red blood cells and nucleated cells: Y. Tan, et al.; Glycoconj. J. 27, 427 (2010), Abstract;
First quantitative assay of alpha-Gal in soft tissues: presence and distribution of the epitope before and after cell removal from xenogeneic heart valves: F. Naso, et al.; Acta Biomater. 7, 1728 (2010), Abstract;
The retention of extracellular matrix proteins and angiogenic and mitogenic cytokines in a decellularized porcine dermis: D.M. Hoganson, et al.; Biomaterials 31, 6730 (2010), Abstract;
A novel method to display [gal alpha1, 3 gal] antigens on human leukemic cells for preparation of anti-leukemia vaccines: K.J. Posekany, et al.; Anticancer Res. 29, 2387 (2009), Abstract;
Increased immunogenicity of human immunodeficiency virus gp120 engineered to express Galalpha1-3Galbeta1-4GlcNAc-R epitopes: U. Abdel-Motal, et al.; J. Virol. 80, 6943 (2006), Abstract; Full Text
Lack of Galactose-alpha-1,3-Galactose Expression on Porcine Endothelial Cells Prevents Complement-Induced Lysis but Not Direct Xenogeneic NK Cytotoxicity: B.C. Baumann, et al.; J. Immunol. 172, 6460 (2004), Abstract;
Differential expression of Galalpha1,3Gal epitopes on fetal and adult porcine hematopoietic cells: S. Gojo, et al.; Xenotransplantation 9, 297 (2002), Abstract; Full Text
Expression of alpha-gal epitopes on HeLa cells transduced wtih adenovirus containing alpha-1,3galactosyltransferase cDNA: L. Deriy, et al.; Glycobiology 12, 135 (2002), Abstract;
Remodeling of the Major Pig Xenoantigen by N-Actetylglucosaminyltransferase III in Transgenic Pig: S. Miyagawa, et al.; J. Biol. Chem. 276, 39310 (2001), Abstract; Full Text
Synthesis of α-gal epitopes (Galα1-3Galβ1-4GlcNAc-R) on human tumor cells by recombinant α1,3galactosyltransferase produced in Pichia pastoris: Z.C. Chen, et al.; Glycobiology 11, 577 (2001), Abstract; Full Text
The alpha-gal epitope (Gal alpha 1-3Gal beta 1-4GlcNAc-R) in xenotransplantation: U. Galili; Biochimie 83, 557 (2001), Abstract;
Differential expression of alpha-Gal epitopes on pig and mouse organs: M. Tanemura & U. Galili; Transplant. Proc. 32, 843 (2000), Abstract;
Differential immune responses to alpha-gal epitopes on xenografts and allografts: implications for accommodation in xenotransplantation: M. Tanemura, et al.; J. Clin. Invest. 105, 301 (2000), Abstract;
Mechanism of delayed rejection in transgenic pig-to-primate cardiac xenotransplantation: R.H. Chen, et al.; J. Surg. Res. 90, 119 (2000), Abstract;
Xenotransplantation: in vitro analysis of synthetic alpha-galactosyl inhibitors of human anti-Galalpha1-->3Gal IgM and IgG antibodies: R. Rieben, et al.; Glycobiology 10, 141 (2000), Abstract;
alpha-Gal Oligosaccharides: Chemistry and Potential Biomedical Application: A. Janczuk, et al.; Curr. Med. Chem. 6, 155 (1999), Abstract;
Regulation of natural killer cell-mediated swine endothelial cell lysis through genetic remodeling of a glycoantigen: S. Miyagawa, et al.; J. Biochem. 126, 1067 (1999), Abstract;
A sensitive assay for measuring alpha-Gal epitope expression on cells by a monoclonal anti-Gal antibody: U. Galili, et al.; Transplantation 65, 1129 (1998), Abstract;

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