Biotin-X, succinimidyl ester

Product ID: M0783



Unit SizePriceQuantity 
50mg
$67.35
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Description

This reactive biotin derivative contains an aminohexanoyl spacer group (termed "X") between biotin and the binding site for proteins, nucleic acids, or other biological molecules which helps to reduce potential quenching effects of fluorophores attached to the analyte molecule, since biotin binds to "deep" binding sites in avidin or streptavidin.

The extra linking arm of this biotin derivative makes it more accessible for binding, and improves a variety of assays employing biotin-avidin or biotin-streptavidin systems. This amine reactive (succinimidyl ester, SE) derivative can be readily coupled to primary or secondary amines of analyte compounds or proteins under mild conditions. Biotin is a commonly used hapten that can be detected by using its strong affinity for the proteins avidin (from egg white) or streptavidin. Many avidin or streptavidin conjugates are available that have been fluorescently labeled or are conjugated to an antibody or other detection reagent. This biotin labeling compound has been used in many such detection schemes for peptides, proteins, organelle components, monoclonal antibody analyses, oligonucleotide and microbead labelings. See references below for further information on the use of biotin labeling.

Technical Data
SKU M0783
CAS Number 72040-63-2
Unit Size 50mg
Alternative Names Biotin-X, SE; Biotinamidohexanoic acid N-hydroxysuccinimide ester; 6-((biotinoyl)amino)hexanoic acid, succinimidyl ester; biotinamidocaproate, N-hydroxysuccinimidyl ester
Molecular Formula C₂₀H₃₀N₄O₆S
Molecular Weight 454.55
Soluble In DMSO, H₂O
Storage Conditions -20C, Desiccated

References and Citations

References:

  • "Oxazolidinones mechanism of action: inhibition of the first peptide bond formation." Patel U, Yan YP, Hobbs FW Jr, Kaczmarczyk J, Slee AM, Pompliano DL, Kurilla MG, Bobkova EV. J Biol Chem 276, 37199-205 (2001)
  • "In-situ monitoring of protein labeling reactions by matrix-assisted laser desorption/ionization mass spectrometry." Lu J, Zenobi R. Fresenius J Anal Chem 366, 3-9 (2000)
  • "Peptide biotinylation with amine-reactive esters: differential side chain reactivity." Miller BT, Collins TJ, Rogers ME, Kurosky A. Peptides 18, 1585-1595 (1997)
  • "Phorbol 12-myristate 13-acetate down-regulates Na,K-ATPase independent of its protein kinase C site: decrease in basolateral cell surface area." Beron J, Forster I, Beguin P, Geering K, Verrey F. Mol Biol Cell 8, 387-398 (1997)
  • "Identification and characterization of O-biotinylated hydroxy amino acid residues in peptides." Miller BT, Rogers ME, Smith JS, Kurosky A. Anal Biochem 219, 240-248 (1994)
  • "The biotin/avidin-mediated microtiter plate lectin assay with the use of chemically modified glycoprotein ligand." Duk M, Lisowska E, Wu JH, Wu AM. Anal Biochem 221, 266-272 (1994)
  • "In Vitro Synthesis of Biotinylated RNA Probes from A-T Rich Templates: Problems and Solutions." Luehrsen KR, Baum MP. Biotechniques 5, 660 (1987)
  • "Novel biotinylated nucleotide--analogs for labeling and colorimetric detection of DNA." Gebeyehu G, Rao PY, SooChan P, Simms DA, Klevan L. Nucleic Acids Res 15, 4513-4534 (1987)
  • "Homogeneous functional insulin receptor from 3T3-L1 adipocytes. Purification using N alpha B1-(biotinyl-epsilon-aminocaproyl)insulin and avidin-sepharose." Kohanski RA, Lane MD. J Biol Chem 260, 5014-5025 (1985).
  • "Immunogenicity of biotinylated hapten-avidin complexes." Scott D, Nitecki DE, Kindler H, Goodman JW. Mol Immunol 21, 1055-1060 (1984)
  • "Avidin-biotin affinity chromatography: application to the isolation of human placental insulin receptor." Finn FM, Titus G, Horstman D, Hofmann K. Proc Natl Acad Sci U S A 81, 7328-7332 (1984)
  • "Rapid and sensitive colorimetric method for visualizing biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bio-blots." Leary JJ, Brigati DJ, Ward DC. Proc Natl Acad Sci U S A 80, 4045-4049 (1983)
  • "Avidin binding of carboxyl-substituted biotin and analogues." Hofmann K, Titus G, Montibeller JA, Finn FM. Biochemistry 21, 978-984 (1982).
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