【Protein A-HRP】Southernbiotech Protein A-HRP

蛋白A(Protein A)-HRP

蛋白A(Protein A)是最初在細菌金黃色葡萄球菌(bacterium Staphylococcus aureus)的細胞壁中發現的42kD表面蛋白 (surface protein)。由於其結合免疫球蛋白(immunoglobulins)的能力，它被廣泛用於生物化學研究(biochemical research)和工業(industry)。它由五個同源的Ig結合結構域(homologous Ig-binding domains)組成，折疊成三螺旋束(three-helix bundle)。每個結構域能夠結合來自許多哺乳動物物種的蛋白質，最值得注意的是IgG(immunoglobulins)。它結合大多數免疫球蛋白的Fc區內的重鏈(heavy chain)。將蛋白A標誌HRP (貨號7300-05 )，可應用於檢測一抗，例如ELISA，ELISPOT，IHC或Western印跡 (Western blotting) 。 IP隨後進行Western blotting應用，HRP蛋白A將避免IgG重鏈/輕鏈(heavy/light chain)問題，因為它僅識別其天然形式的IgG，並且用於IP靶標的抗體通常與免疫沉澱物一起煮沸並變性。

產品介紹: Protein A-HRP，具HRP標誌。針對Binds the Fc portion of human IgG1, IgG2, and IgG4 as well as mouse IgG2aand IgG2b; also binds rabbit, porcine, guinea pig, and canine IgG具特異性。來源為Staphylococcus aureus。緩衝液配方在50% Glycerol/50% Phosphate buffered saline, pH 7.4。結構Monomeric protein lacking cysteine residues; Mr 42 kDa

Source	Staphylococcus aureus
Specificity	Binds the Fc portion of human IgG₁, IgG₂, and IgG₄ as well as mouse IgG_2aand IgG_2b; also binds rabbit, porcine, guinea pig, and canine IgG
Buffer Formulation	50% Glycerol/50% Phosphate buffered saline, pH 7.4
Volume	1.0 mL
Storage & Handling	2-8°C Please refer to product specific SDS
Applications	ELISA – Quality tested ^1-7 Purification WB ⁸ IP
Recommended Dilutions	Please refer to product specific Technical Bulletin

References

Sondgeroth K, Blitvich B, Blair C, Terwee J, Junge R, Sauther M, et al. Assessing flavivirus, lentivirus, and herpesvirus exposure in free-ranging ring-tailed lemurs in southwestern Madagascar. J Wildl Dis. 2007;43:40-7. (ELISA)
Wycoff KL, Belle A, Deppe D, Schaefer L, Maclean JM, Haase S, et al. Recombinant anthrax toxin receptor-Fc fusion proteins produced in plants protect rabbits against inhalational anthrax. Antimicrob Agents Chemother. 2011;55:132-9. (ELISA)
Duthie MS, Truman RW, Goto W, O’Donnell J, Hay MN, Spencer JS, et al. Insight toward early diagnosis of leprosy through analysis of the developing antibody responses of Mycobacterium leprae-infected armadillos. Clin Vaccine Immunol. 2011;18:254-9. (ELISA)
Arzola L, Chen J, Rattanaporn K, Maclean JM, McDonald KA. Transient co-expression of post-transcriptional gene silencing suppressors for increased in planta expression of a recombinant anthrax receptor fusion protein. Int J Mol Sci. 2011;12:4975-90. (ELISA)
Karuppanan K, Duhra-Gill S, Kailemia MJ, Phu ML, Lebrilla CB, Dandekar AM, et al. Expression, purification, and biophysical characterization of a secreted anthrax decoy fusion protein in Nicotiana benthamiana. Int J Mol Sci. 2017;18:89. (ELISA)
Xiong Y, Li Q, Kailemia MJ, Lebrilla CB, Nandi S, McDonald KA. Glycoform modification of secreted recombinant glycoproteins through kifunensine addition during transient vacuum agroinfiltration. Int J Mol Sci. 2018;19:890. (ELISA)
Sukenik SC, Karuppanan K, Li Q, Lebrilla CB, Nandi S, McDonald KA. Transient recombinant protein production in glycoengineered Nicotiana benthamiana cell suspension culture. Int J Mol Sci. 2018;19:1205. (ELISA)
Naskar P, Puri N. Phosphorylation of SNAP-23 regulates its dynamic membrane association during mast cell exocytosis. Biol Open. 2017;6:1257-69. (WB)