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Anti-Alpha-Galactosyl IgM Human ELISA

  • Regulatory status:RUO
  • Type:Capture ELISA, HRP-labelled antibody
  • Other names:Anti-Alpha-Galactosyl Antibody
  • Species:Human
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Cat. No. Size Price


RD199178110R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Capture ELISA, HRP-labelled antibody

Applications

Serum, Plasma-EDTA, Plasma-Heparin, Plasma-Citrate

Sample Requirements

5 ul/well

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the complete kit at 2 – 8° C. Under these conditions, the kit is stable until the expiration date (see label on the box).

Calibration Curve

Calibration Range

3.13 – 100 U/mL

Limit of Detection

1.35 U/ml

Intra-assay (Within-Run)

n = 8; CV = 2.9%

Inter-assay (Run-to-Run)

n = 5; CV = 6.4%

Spiking Recovery

90,90%

Dilution Linearity

99,00%

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3 hours
  • The kit measures IgM anti-alpha-galactosyl antibodies in human serum and plasma (EDTA, citrate, heparin)
  • Assay format is 96 wells
  • Calibrator is human serum based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Autoimmunity, Immune Response, Infection and Inflammation, Immunology, Oncology, Transplantation

Summary

Natural antibodies circulate in serum of healthy humans naturally, without previous immunization. They can be directed against the individual’s own antigens as well as against foreign antigens. The repertoire of natural antibodies is encoded by germ-line genes and is not subjected to recombination. Natural antibodies are polyreactive and react with low affinity but high avidity. Among the natural antibodies directed against saccharide antigens, the best known are:

  1. isohemagglutinins (anti-A, anti-B) which prevent the transfusion of allogeneic blood and allotransplan­tation;
  2. xenoagglutinins (80% of the repertoire of human xenoreactive natural antibodies is specific for the terminal α-galactose determinant) which have traditionally been detected by agglutination test with rabbit or porcine erythrocytes. The epitope against which they are directed was identified as Galα1–3Galβ1–4GlcNAc-R. This epitope is present in cell membranes of mammals with the exception of humans and Old World primates in which the gene encoding for α-1,3-galactosyltran­sferase was inactivated during evolution. This epitope is also present in lipopolysaccharides and capsular polysaccharides of various gramnegative bacteria colonizing the gastrointestinal tract of humans.

In human serum, natural anti-α-galactosyl antibodies (anti-α-Gal) constitute approximately 4 –8 % of total serum IgM, approx. 1 – 2 % of total serum IgG, and they can also be found as the IgA isotope in serum, saliva, milk, colostrum and vaginal washings. About 1 % of circulating B lymphocytes in adults is capable of producing these antibodies. Their production is thought to be induced postnatally after antigenic stimuli by intestinal microflora. The biological roles of natural antibodies are thought to be protection against infectious agents, particularly at the mucosal surface, effector functions of the immune system, e.g. in removing senescent or otherwise altered cells and physiologically degraded molecules, and regulation of immune responses, particularly autoimmune responses. Moreover, the presence of anti-α-galactosyl antibodies in humans represents an important obstacle to xenotransplan­tations of porcine grafts since these antibodies participate in their rejection. Natural antibodies also play an important role in malignant processes, and they have potential to be used in treatment of tumors that express these (α-Gal) antigens (e.g. breast cancer).

Areas of investigation: Immunology, Immune Response, Autoimmunity, Infection and Inflammation, Transplantation, Oncology

Product References (3)

References

  • Hamanova M, Chmelikova M, Nentwich I, Thon V, Lokaj J. Anti-Gal IgM, IgA andIgG natural antibodies in childhood. Immunol Lett. 2015 Mar;164(1):40-3. doi:10.1016/j.imlet.2015.02.001. Epub 2015 Feb 12. PubMed PMID: 25684746. See more on PubMed
  • Kralickova P, Kuhnova J, Soucek O, Vodarek P, Zak P, Simkovic M, Motyckova M, Smolej L, Mala E, Andrys C, Krejsek J, Thon V. Antibodies against PneumococcalCapsular Polysaccharides and Natural Anti-Galactosyl (Alpha-Gal) in Patients withHumoral Immunodeficiencies. J Immunol Res. 2017;2017:7304658. doi:10.1155/2017/7304658. Epub 2017 Dec 17. PubMed PMID: 29392143; PubMed CentralPMCID: PMC5748103. See more on PubMed
  • Tasaki M, Saito K, Nakagawa Y, Imai N, Ito Y, Aoki T, Kamimura M, Narita I,Tomita Y, Takahashi K. Acquired Downregulation of Donor-Specific AntibodyProduction After ABO-Incompatible Kidney Transplantation. Am J Transplant. 2017Jan;17(1):115-128. doi: 10.1111/ajt.13937. Epub 2016 Jul 26. PubMed PMID:27343838. See more on PubMed
Summary References (22)

References to Natural Antibody

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  • Avrameas S, Guilbert B, Mahana W, Matsiota P, Ternynck T. Recognition of self and non-self constituents by polyspecific autoreceptors. Int Rev Immunol. 1988 Mar;3 (1-2):1-15
  • Castronovo V, Colin C, Parent B, Foidart JM, Lambotte R, Mahieu P. Possible role of human natural anti-Gal antibodies in the natural antitumor defense system. J Natl Cancer Inst. 1989 Feb 1;81 (3):212-6
  • Coutinho A, Kazatchkine MD, Avrameas S. Natural autoantibodies. Curr Opin Immunol. 1995 Dec;7 (6):812-8
  • Dighiero G, Lymberi P, Guilbert B, Ternynck T, Avrameas S. Natural autoantibodies constitute a substantial part of normal circulating immunoglobulins. Ann N Y Acad Sci. 1986;475:135-45
  • Galili U. Evolution and pathophysiology of the human natural anti-alpha-galactosyl IgG (anti-Gal) antibody. Springer Semin Immunopathol. 1993;15 (2-3):155-71
  • Galili U, Anaraki F, Thall A, Hill-Black C, Radic M. One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody. Blood. 1993 Oct 15;82 (8):2485-93
  • Galili U, Clark MR, Shohet SB, Buehler J, Macher BA. Evolutionary relationship between the natural anti-Gal antibody and the Gal alpha 1----3Gal epitope in primates. Proc Natl Acad Sci U S A. 1987 Mar;84 (5):1369-73
  • Galili U, LaTemple DC. Natural anti-Gal antibody as a universal augmenter of autologous tumor vaccine immunogenicity. Immunol Today. 1997 Jun;18 (6):281-5
  • Galili U, Macher BA, Buehler J, Shohet SB. Human natural anti-alpha-galactosyl IgG. II. The specific recognition of alpha (1----3)-linked galactose residues. J Exp Med. 1985 Aug 1;162 (2):573-82
  • Galili U, Mandrell RE, Hamadeh RM, Shohet SB, Griffiss JM. Interaction between human natural anti-alpha-galactosyl immunoglobulin G and bacteria of the human flora. Infect Immun. 1988 Jul;56 (7):1730-7
  • Galili U, Swanson K. Gene sequences suggest inactivation of alpha-1,3-galactosyltransferase in catarrhines after the divergence of apes from monkeys. Proc Natl Acad Sci U S A. 1991 Aug 15;88 (16):7401-4
  • Galili U, Wigglesworth K, Abdel-Motal UM. Intratumoral injection of alpha-gal glycolipids induces xenograft-like destruction and conversion of lesions into endogenous vaccines. J Immunol. 2007 Apr 1;178 (7):4676-87
  • Good AH, Cooper DK, Malcolm AJ, Ippolito RM, Koren E, Neethling FA, Ye Y, Zuhdi N, Lamontagne LR. Identification of carbohydrate structures that bind human antiporcine antibodies: implications for discordant xenografting in humans. Transplant Proc. 1992 Apr;24 (2):559-62
  • Hamadeh RM, Galili U, Zhou P, Griffiss JM. Anti-alpha-galactosyl immunoglobulin A (IgA), IgG, and IgM in human secretions. Clin Diagn Lab Immunol. 1995 Mar;2 (2):125-31
  • Manches O, Plumas J, Lui G, Chaperot L, Molens JP, Sotto JJ, Bensa JC, Galili U. Anti-Gal-mediated targeting of human B lymphoma cells to antigen-presenting cells: a potential method for immunotherapy using autologous tumor cells. Haematologica. 2005 May;90 (5):625-34
  • McMorrow IM, Comrack CA, Sachs DH, DerSimonian H. Heterogeneity of human anti-pig natural antibodies cross-reactive with the Gal(alpha1,3)Galactose epitope. Transplantation. 1997 Aug 15;64 (3):501-10
  • Ochsenbein AF, Zinkernagel RM. Natural antibodies and complement link innate and acquired immunity. Immunol Today. 2000 Dec;21 (12):624-30
  • Parker W, Bruno D, Holzknecht ZE, Platt JL. Characterization and affinity isolation of xenoreactive human natural antibodies. J Immunol. 1994 Oct 15;153 (8):3791-803
  • STARZL TE, MARCHIORO TL, HOLMES JH, HERMANN G, BRITTAIN RS, STONINGTON OH, TALMAGE DW, WADDELL WR. RENAL HOMOGRAFTS IN PATIENTS WITH MAJOR DONOR-RECIPIENT BLOOD GROUP INCOMPATIBILITIES. Surgery. 1964 Feb;55:195-200
  • Ternynck T, Avram
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