SSI Antibodies expands the antibody portfolio with a number of interesting antibodies.
HAH 002-01 Anti Butyrylcholinesterase clone 3E8
SSI Antibodies is delighted to announce that our customers can now purchase the monoclonal antibody HAH 002-01 Anti Butyrylcholinesterase clone 3E8 directly from Statens Serum Institut, where the antibody was developed by scientists back in the 1980’s (Brock A et al. 1990).
Butyrylcholinesterase (BChE) has gained huge interest from scientists after the US Department of Defence allocated millions of dollars for the purification of pure human BChE to use as a scavenger for protection against the toxicity of nerve agents that target the enzymatic activity of acetylcholinesterase, which terminates neurotransmission by hydrolyzing the neurotransmitter acetylcholine (Masson and Lockridge 2010). HAH 002-01 Anti Butyrylcholinesterase is now frequently used for detection of nerve agent exposure by a method that combines immunomagnetic separation and liquid chromatography tandem mass spectrometry to quantification of butyrylcholinesterase nerve agent adducts in human serum (Sporty JL et al 2010, Carter MD et al. 2014 and Pantazides BG et al. 2014).
Moreover, HAH 002-01 Anti Butyrylcholinesterase is interesting with respect to purification of BChE for use as anti-cocaine medication, since BChE is one of the major cocaine-metabolizing enzymes in humans and the principal cocaine hydrolase in human serum (Yang W et al 2009).
- Brock A, Mortensen V, Rasmussen Loft AG, Nørgaard-Pedersen B. Enzyme Immunoassay of Human Cholinesterase (EC 184.108.40.206) Comparison of immunoreactive substance concentration with catalytic activity concentration in randomly selected serum samples from healthy individuals. J Clin Chem Biochem. 1990:28(4):221-4.
- Carter MD, Crow BS, Pantazides BG, Watson CM, DeCastro BR, Thomas JD, Blake TA, Johnson RC. Profiling cholinesterase adduction: a high-throughput prioritization method for organophosphate exposure samples.J Biomol Screen. 2014 Feb;19(2):325-30. doi: 10.1177/1087057113497799. Epub 2013 Aug 16. PMID: 23954929
- Masson P, Lockridge O. Butyrylcholinesterase for protection from organophosphorus poisons; catalytic complexities and hysteretic behavior. Arch Biochem Biophys. 2010:15:494(2): 107.
- Pantazides BG, Watson CM, Carter MD, Crow BS, Perez JW, Blake TA, Thomas JD, Johnson RC. An enhanced butyrylcholinesterase method to measure organophosphorus nerve agent exposure in humans. Anal Bioanal Chem. 2014 Aug;406(21):5187-94. doi: 10.1007/s00216-014-7718-7. Epub 2014 Mar 7. PMID: 24604326
- Sporty JL, Lemire SW, Jakubowski EM, Renner JA, Evans RA, Williams RF, Schmidt JG, van der Schans MJ, Noort D, Johnson RC. Immunomagnetic separation and quantification of butyrylcholinesterase nerve agent adducts in human serum. Anal Chem. 2010:82(15):6593-600.
- Yang W, Pan Y, Zheng F, Cho H, Tai HH, Zhan CG. Free-Energy Perturbation Simulation on Transition States and Redesign of Butyrylcholinesterase Biophys J. 2009 Mar 4; 96(5): 1931–1938.
SSI-HYB 364-02 Anti Mouse Major Urinary Protein 3 (MUP3) clone SSI-7B10
SSI Antibodies introduces a new antibody, SSI-HYB 364-02 against the murine major urinary protein 3 (MUP3). MUPs are androgen-regulated pheromone-binding proteins, that are synthesized in the liver, secreted in the bloodstream and excreted into the urine.
Mice are among the most frequently used laboratory animals and allergy to them constitutes an occupational hazard. Approximately 20 % of the personnel engaged in work with laboratory animals have acquired symptoms of allergy (Renström A et al). MUPs are very important allergens and they are quantitatively the major protein in urine of fertile male mice as they constitute approximately 30% of the total protein content excreted in the urine (Beynon RJ and Hurst JL 2004). Moreover, exposure to mouse MUP allergens is associated with and a potentially important trigger of asthma symptoms (Salo PM el al 2009 and Sheehan WJ et al 2009). SSI-HYB 364-02 is suitable for use in an inhibition ELISA for detection of MUP3.
- Beynon, R.J. and Hurst, J.L. (2004). Urinary proteins and the modulation of chemical scents in mice and rats. Peptides 25, 1553-1563.
- Renström, A., Karlsson, A.-S., Malmberg, P., Larsson, P.H., van Hage-Hamsten, M. (2001). Working with male rodents may increase risk of allergy to laboratory animals. Allergy 56,
- Salo PM, Jaramillo R, Cohn RD, London SJ, Zeldin DC. Exposure to mouse allergen in U.S. homes associated with asthma symptoms.
Environ Health Perspect. 2009 Mar;117(3):387-91. doi: 10.1289/ehp.11847. Epub 2008 Oct 6.
- Sheehan WJ, Rangsithienchai PA, Muilenberg ML, Rogers CA, Lane JP, Ghaemghami J, Rivard DV, Otsu K, Hoffman EB, Israel E, Gold DR, Phipatanakul W. Mouse allergens in
urban elementary schools and homes of children with asthma. Ann Allergy Asthma Immunol. 2009 Feb;102(2):125-30. doi: 10.1016/S1081-1206(10)60242-6. PMID:19230463.
SSI-HYB 353-01 Anti Ro60 clone SSI-34C4, SSI-HYB 353-02 Anti Ro60 clone SSI-39B4, SSI-HYB 353-05 Anti Ro60 clone SSI-7G8 and SSI-HYB 353-06 Anti Ro60 clone SSI-7G7
Within the field of autoimmunology, SSI Antibodies introduces four new antibodies, SSI-HYB 353-01, SSI-HYB 353-02, SSI-HYB 353-05 and SSI-HYB 353-06 against Ro60, which is a 60 kDa ring-shaped protein with two overlapping RNA binding sites that binds misfolded RNAs and contributes to the cellular RNA quality control program (Sims S et al 2009). Ro60 is also known as the SSA antigen associated with the autoimmune disorder Sjögren’s Syndrome and it is a major target of autoantibodies in patients suffering from the rheumatic diseases systemic lupus erythematosus, subacute cutaneous lupus erythematosus and neonatal lupus erythematosus. SSI-HYB 353-01, SSI-HYB 353-02, SSI-HYB 353-05 and SSI-HYB 353-06 recognize a conformational epitope (Ødum et al 2016) and can be used for detection of Ro-60 in a sandwich ELISA. All antibodies are useful for immunoblotting and SSI-HYB 353-02, SSI HYB 353-05 and SSI-HYB 353-06 are also for immunofluorescent cell staining of Ro60.
- Sim S, Weinberg DE, Fuchs G, Choi K, Chung J, Wolin SL. The subcellular distribution of an RNA quality control protein, the Ro autoantigen, is regulated by noncoding Y RNA binding. Mol Biol Cell. 2009 Mar;20(5):1555-64. doi: 10.1091/mbc.E08-11-1094. Epub 2008 Dec 30. PMID: 19116308
- Ødum Nielsen I, Hartwig Trier N, Friis T, Houen G. Characterization of continuous monoclonal antibody epitopes in the N-terminus of Ro60. Biopolymers. 2016 Jan;106(1):62-71. doi: 10.1002/bip.22758. PMID: 26506479