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Protein Labeling Kit, BioAssay(TM) (Biotin)

Cat no: B1750-49A

Protein Labeling Kit, BioAssay(TM) (Biotin)

Protein Labeling Kit, BioAssay(TM) (Biotin) is designed for the simple and fast labeling of proteins with biotin. The kit is ideally suited to label antibodies, hormones, or other proteins as well as other macromolecules containing primary amino groups. Labeled proteins can be used in a number of applications, such as immunological assays, fluorescence microscopy, investigation of protein-protein interactions, etc. The labeling reagent, BLA (Biotin Long Arm) NHS, reacts with a primary amine on the protein, forming a covalent amide bond with a spacer arm between the biotin and the protein. Incorporation of the label is mainly accom- plished through reaction with primary amines on lysine residues or terminal amino groups. The linkage between biotin and the protein produced with this reagent is stable, with no significant loss of the label during storage.\n\nEach kit contains all the components needed for at least five labeling reactions (up to 1mg of protein per reaction)\n\nKit Components:\nLabeling Reagent (N-hydroxysuccinimidyl-6-(biotin amido) hexanoate)\nReagent Solvent\nReaction Buffer\nStop Reagent\nGel Filtration Slurry\n5x1ml Spin Columns\n5x2ml Collection Tubes\nAgarose Avidin D Slurry\n\nStorage and Stability:\nStore powder at 4 degrees C, liquid at -20 degrees C. Store other components at 4 degrees C. Stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

B1750-49A

Size

1Kit

References

1. Garbern JC et al. 2010. Delivery of basic fibroblast growth factor with a pH-responsive, injectable hydrogel to improve angiogenesis in infracted myocardium. Biomaterials. 32:2407-16. Wu J et al. 2009. 2. Identification of binding peptides of the ADAM15 disintegin domain using phage display. J. Biosci. 34(2):1-8. Tabata H, Kanatani S, Nakajima K. 2009. Differences of migratory behavior between direct progeny and basal progenitors in the developing cerebral cortex. Cerebral Cortex. Advanced Publication. doi:10.1093/cercor/bhn227 Guglielmo-Viret V, Thullier P. 2007. 3. Comparison of an electrochemiluminescence assay in plate format over a colorimetric ELISA, for the detection of ricin B chain (RCA- B). J Immunol Methods. 328:70-78. Kerr LE, Birse-Archbold J-LA, Short DM, McGregor AL, Heron I, MacDonald DC, Thompson J, Carlson GJ, Kelly JS, McCulloch J, Sharkey J. 2007. 4. Nucleophosmin is a novel Bax chaperone that regulates apoptotic cell death. Oncogene. 26:2554-62. Zou K, Yamaguchi H, Akatsu H, Sakamoto T, Ko M, Mizoguchi K, Gong J-S, Yu W, Yamamoto T, Kosaka K, Yanagisawa K, Michikawa M. 2007. 5. Angiotensin-converting enzyme converts amyloid b-protein 1-42 (Ab1-42) to Ab1-40, and its inhibition enhances brain Ab deposition. J Neurosci. 27(32):8628-35. Hatta J, Oshihisa Hatta T, Moritake K, Otani H. 2006. 6. Heavy water inhibiting the expression of transforming growth factor-1 and the development of kaolin-induced hydrocephalus in mice. J Neuroserg. 104:251-58. Ohta S, Bahrun U, Shimazu R, Matsushita H, Fukudome K, Kimoto M. 2006. 7. Induction of long-term lipopolysaccharide tolerance by an agonistic monoclonal antibody to the Toll-Like Receptor 4/MD-2 complex. Clin. Vaccine Immunol. 13(10):1131-6. Pathak S, Cao E, Davidson MC, Jin S, Silva GA. 2006. 8. Quantum dot applications to neuroscience: New tools for probing neurons and glia. J Neurosci. 26(7):1893-5. ProtOnTM Fluorescein: Chen Z et al. 2011. 9. Synergism of human amnion-derived multipotent progenitor (AMP) cells and a collagen scaffold in promoting brain wound recovery: Pre-clinical studies in an experimental model of penetrating ballistic-like brain injury. Brain Res. 1368:71-81. Cook AF et al. 2009. 10. Face-specific binding of prothrombin fragment 1 and human serum albumin to inorganic and urinary calcium oxalate monohydrate crystals. BJU Int. 103(6):826-35. Elliott RMA et al. 2009. 11. Effects of HSPA8, an evolutionarily conserved oviductal protein, on boar and bull spermatozoa. Reproduction. 137:191-203. Huang L, Adachi T, Shimizu Y, Goto Y, Toyama J, Tanaka H, Akashi R, Sawaguchi A, Iwata H, Haga T. 2008, 12. Characterization of lectin isolated from Momordica charantia seed as a B cell activator. Immunol Letters. 121:148-56. Ip JE, Wu Y, Huang J, Zhang L, Pratt RE, Dzau VJ. 2007. 13. Mesenchymal stem cells utilize Integrin b1 not CXCR4 for myocardial migration and engraftment. Mol. Biol. Cell. 18(8):2873-82. Prathalingam NS, Hold WV, Revell SG, Mirczuk S, Fleck RA, Watson PF. 2006. 14. Impact of antifreeze proteins and antifreeze glycoproteins on bovine sperm during freeze- thaw. Theriogenol. 66:1894-1900. Sun Y-X, Fang M, Wang J, Cooper CR, Pienta KJ, Taichman RS. 2007. 15. Expression and activation of avb3 Integrins by SDF-1/CXC12 Increases the aggressiveness of prostate cancer cells. The Prostate. 67:61-73. Wu Y et al. 2006. 16. Essential role of ICAM-1/CD18 in mediating EPC recruitment, angiogenesis, and repair to the infracted myocardium. Circ. Res. 99:315-22. Yoshida K, Inoue I. 2004. 17. Peptide binding to Geminin and inhibitory for DNA replication. Biochem. Biophys. Res. Comm. 317:218-22.

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