Product Name :
Donkey Chicken IgY, conjugated with Agarose
Description :
| Product Type Secondary antibodies | Units 1.0 ml bed volume | Host Donkey
Background :
A donkey was immunized with purified chicken IgY. Antibodies were isolated from immune sera using affinity chromatography and conjugated to N- hydroxysuccinimide (NHS)-activated agarose beads. Beads were washed extensively after the blocking of the residual NHS sites.
Source :
Product :
Gel; 1 ml settled gel Product Form: Immunoprecipitation Gel Formulation: Phosphate buffered saline‚ pH 7.2 with 0.075% sodium azide Purification Method: Egg-yolk derived IgY Affinity Purified Concentration: N/A
Specificity :
Applications :
The specific activity of the anti-IgY-agarose was determined by applying 2.7 mg IgY in 24 ml PBS (0.1 mg/ml) to 1.0 ml bed volume of agarose. Two ml aliquots were collected. The total amount of IgY that bound to the column was calculated. For this lot, 1.3 mg IgY bound per ml agarose.
Storage :
Product should be stored at 4-8°C. DO NOT FREEZE
Caution :
This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals. It may contain hazardous ingredients. Please refer to the Safety Data Sheets (SDS) for additional information and proper handling procedures. Dispose product remainders according to local regulations.This datasheet is as accurate as reasonably achievable, but our company accepts no liability for any inaccuracies or omissions in this information.
References :
1. Hall, Sarah E., Song Luo, Anne E. Hall, and Daphne Preuss, 2005, Differential Rates of Local and Global Homogenization in Centromere Satellites From Arabidopsis Relatives. Genetics: 170(4): 1913–1927. 2. Song, M-G and M. Kiledjian, 2007. 3′ Terminal oligo U-tract-mediated stimulation of decapping. RNA, 13:2356-2365. 3. Taylor, A.I., H.J. Gould, B.J. Sutton and R.A. Calvert. 2008. Avian IgY Binds to a Monocyte Receptor with IgG-like Kinetics Despite an IgE-like Structure. J. Biol. Chem. 283: 16384-16390. 4. S-C. Lo and M. Hannink. 2008. PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria. Experimental Cell Research 314: 1789-1803. 5. C. Butkinaree, W.D. Cheung, S. Park, K. Park, M. Barber and G.W. Hart, 2008. Characterization of Beta-N-Acetylglucosaminidase Cleavage by Caspase-3 during Apoptosis. J. Biol. Chem., 283:23557-23566. 6. Slawson,C. Lakshmanan, T., Knapp, S. and Hart, G.W., 2008, A Mitotic GlcNAcylation/Phosphorylation Signaling Complex Alters the Posttranslational State of the Cytoskeletal Protein Vimentin. Mol. Biol. Cell 19:4130-4140. 7. McMichael, Brooke K., Cheney, Richard E., and Beth S. Lee. 2010. Myosin X Regulates Sealing Zone Patterning in Osteoclasts through Linkage of Podosomes and Microtubules. J Biol. Chem. 285:9506-9515. 8. Hale, C.R., Sonali, M., Elmore, J., Pfister, N., Compton, M., Olson S., Resch, A.M., Glover III, C.V.C., Graveley B.R., Terns, R.M., and M.P. Terns. 2012. Essential Features and Rational Design of CRISPR RNAs that Function with the Cas RAMP Module Complex to Cleave RNAs. Molecular Cell 45:292-302. 9. Lehman, HL, van Laere SJ, van Golen, CM, Vermeulen PB, Dirix LY and KL van Golen. 2012. Regulation of inflammatory breast cancer cell invasion through Akt1/PKB? phosphorylation of RhoC GTPase. Mol Cancer Res. 10:1306-18. 10. Cheadle L. and T. Biederer. 2012. The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal dynamics and transsynaptic organization. J Cell Biol. 199:985-1001. 11. Dai, L, Taylor, MS, O’Donnell, KA and JD Boeke. 2012. Poly (A) Binding Protein C1 is Essential for Efficient L1 Retrotransposition and Affects L1 RNP Formation. Mol Cell Biol. 32:4323-4336. 12. Joglekar, M, Elbazanti, WO, Weizman, MD, Lehman, HL and van Golen, KL. 2015. Caveolin-1 Mediates Inflammatory Breast Cancer Cell Invasion via the Akt1 Pathway and RhoC GTPase. J. Cell. Biochem 116:923-933. 13. Zhang, Z., Costa, FC, Tan, EP, Bushue, N, DiTacchio, N, Costello, CE, McComb, ME, Whelan, SA, Petersen, KR, and Slawson, C. 2016. O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2? Protein at the A?-Globin Promoter. J. Biol Chem 291:15628-40. 14. Balachandran RS, Heighington CS, Starostina NG, Anderson JW, Owen DL, Vasudevan S, Kipreos ET. 2016. The ubiquitin ligase CRL2ZYG11 targets cyclin B1 for degradation in a conserved pathway that facilitates mitotic slippage. J Cell Biol. 215(2):151-166.
Related websites: https://www.medchemexpress.com/antibodies.html
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