Goat anti-rabbit IgG (H&L) Agarose
| Overview |  SDSProtocol |
See also: Secondary Antibodies, Antibodies and Proteomics
Molecular weight 150000 |
Agarose conjugated antibodies are designed for the rapid and efficient collection of antibodies and proteins, including recombinant fusion proteins, from a complex protein mixture (see protocol). Antibody affinity gels are useful for selection of immunoglobulins and immunoprecipitation of antigens from sera, antisera, ascitic fluid or culture fluid, bacterial and mammalian cell lysates and fusion protein preparations.
Calculators
Common stock solution preparation
Table 1. Volume of appropriate solvent needed to reconstitute specific mass of Goat anti-rabbit IgG (H&L) Agarose to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.
| 0.1 mg | 0.5 mg | 1 mg | 5 mg | 10 mg | |
| 1 mM | 666.667 nL | 3.333 µL | 6.667 µL | 33.333 µL | 66.667 µL |
| 5 mM | 133.333 nL | 666.667 nL | 1.333 µL | 6.667 µL | 13.333 µL |
| 10 mM | 66.667 nL | 333.333 nL | 666.667 nL | 3.333 µL | 6.667 µL |
Molarity calculator
Enter any two values (mass, volume, concentration) to calculate the third.
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Images
Figure 1. Agarose conjugated antibodies are designed for the rapid and efficient collection of antibodies from a complex protein mixture. Antibody affinity gels are useful for selection of immunoglobulins and immunoprecipitation of antigens from sera, antisera, ascitic fluid or culture fluid, bacterial and mammalian cell lysates and fusion protein preparations.
References
View all 4 references: Citation Explorer
Transient conformational modification of immunoglobulin G during purification by protein A affinity chromatography
Authors: Gagnon, P.; Nian, R.; Leong, D.; Hoi, A.
Journal: J Chromatogr A (2015): 136-42
Authors: Gagnon, P.; Nian, R.; Leong, D.; Hoi, A.
Journal: J Chromatogr A (2015): 136-42
Purification of caveolae by affinity two-phase partitioning using biotinylated antibodies and NeutrAvidin-dextran
Authors: Barinaga-Rementeria Ramirez, I.; Abedinpour, P.; Jergil, B.
Journal: Anal Biochem (2004): 17-26
Authors: Barinaga-Rementeria Ramirez, I.; Abedinpour, P.; Jergil, B.
Journal: Anal Biochem (2004): 17-26
Expression screen by enzyme-linked immunofiltration assay designed for high-throughput purification of affinity-tagged proteins
Authors: Kery, V.; Savage, J. R.; Widjaja, K.; Blake, B. K.; Conklin, D. R.; Ho, Y. S.; Long, X.; von Rechenberg, M.; Zarembinski, T. I.; Boniface, J. J.
Journal: Anal Biochem (2003): 255-8
Authors: Kery, V.; Savage, J. R.; Widjaja, K.; Blake, B. K.; Conklin, D. R.; Ho, Y. S.; Long, X.; von Rechenberg, M.; Zarembinski, T. I.; Boniface, J. J.
Journal: Anal Biochem (2003): 255-8
Chromogranin from normal human adrenal glands: purification by monoclonal antibody affinity chromatography and partial N-terminal amino acid sequence
Authors: Wilson, B. S.; Phan, S. H.; Lloyd, R. V.
Journal: Regul Pept (1986): 207-23
Authors: Wilson, B. S.; Phan, S. H.; Lloyd, R. V.
Journal: Regul Pept (1986): 207-23