● Vitamin H; Essential cellular growth factor.¹
● Specific and high affinity binding to avidin (K_D=10^-15 M).^2,3
● Wide application in immunology, diagnostics, affinity chromatography, etc.
● Used to label DNA.⁴


1.  Wagner, A.F.; Folkers, K. (1964) Vitamins and Coenzymes 138-159.
2.  Green, N.M. (1975) Adv. Protein Chemistry 29,85-133.
3.  Roffman, E., et. al. (1986) Biochem. Biophys. Res. Comm. 136, 80.
4.  (1992) Acta Pharm. Fenn. 101, 147.

Storage 0-4 °C.

● Amino reactive biotinylation reagent for preparing biotinylated surfaces or polypeptides.¹
● Immunoassay development.²
● Wide application in molecular biology.³

1.  Wojchowski, D.M., et.al. (1986) J. Immunol Methods 90, 173-177.
2.  Ngo, T.T., et.al. (1982) Applied Biochem. Biotech. 7, 443-454.
3.  Bayer, E.A., Wilchek, M., (1980) Methods Biochem. Anal. 26, 1.

Storage 0-4 °C.

● Water soluble and amino reactive biotinylation reagent.^1,2
● Wide use in immunodiagnostics.
● Solubility:  (DMF:  50 mg/mL);   (Water:  10 mg/mL.)

1.  LaRochelle, W.J., et.al. (1986) J. Immunol. Methods 92, 65-71.
2.  Pantano, P., Kuhr, W. (1993) Anal. Biochem. 65, 623-630.

Storage 0-4 °C.

(+)-Biotin-PFP-ester; (Molbio Ultra, 99+%)
C₁₆H₁₅N₂SO₃F₅;  M_r=410.36; mp 195 °C;  white glistening flakes.

● More reactive and stable than corresponding NHS ester.
● Highly electrophilic leaving group enables direct labeling of nucleotide bases.

Storage 0-4 °C.

● Glycoprotein biotinylation reagent.^1,2
● Carbohydrate reactive.³

1.  Wade, D.P., et.al. (1985) Biochem. J. 229, 785-790.
2.  Lisanti, M.P., et.al. (1989) J. Cell Biol. 109, 2117-2127.
3.  O'Shannessy, D.J., et.al. (1984) Immun. Letters 8, 273-277.

Storage 25 °C.

● Sulfhydryl reactive biotinylation reagent.¹
● Quantitate biotinylation by release of 2-thiopyridine, l_max343 nm, e=8,080 M^-1 cm^-1.²
● Conjugation of biotin through an -S-S- linkage enables cleavage of the adduct by mild reducing reagents, i.e. DTT, TCEP, etc.

1.  Ghebrehiwet, B., et.al. (1988) J. Immunol. Methods 110, 251-260.
2.  Carlsson, J., et.al. (1978) Biochem. J. 173, 723-737.

Storage 0-4 °C.

● N-terminal biotinylation of peptides using EDC·HCl.
● Useful for custom, synthetic modification of substrates.

Storage 25 °C.

● Amino reactive!¹
● Extended chain (22.4 Å) increases avidin binding.²
● Useful for preparing DNA probes.³

1.  Suter, M., et.al. (1986) Immunology Letters 13, 313-316.
2.  Hofman, K., et.al. (1982) Biochemistry 21, 978-984.
3.  Leary, J.J., et.al. (1983) Proc. Nat. Acad. Sci USA 80, 4045-4049.

Storage 0-4 °C.

● Amino reactive and extended (+)-Biotin.¹
● In vivo tumor site Localization.²
● Water soluble!³

1.  Suter, M., et.al. (1986) Immunology Letters 13, 313-316
2.  Hnatowich, D.J., et.al. (1987) J. Nuc. Med. 86, 1294-1302.
3.  Pantano, P.; et.al. (1993) Anal. Chem. 65, 623-630.

Storage 0-4 °C.

● Glycoprotein biotinylation reagent.¹
● Carbohydrate reactive.^2,3

1.  Wade, D.P., et.al. (1985) Biochem. J. 229, 785-790.
2.  Lisanti, M.P., et.al. (1989) J. Cell Biol. 109, 2117-2127.
3.  O'Shannessy, D.J., et.al. (1984) Immun. Letters 8, 273-277.

Storage 0-4 °C.

● Super Long Chain (+)-Biotin derivative.
● N-terminal biotinylation of peptides.
● For long chain synthetic modification of substrates in organic media.

Storage 25 °C.

● Amino reactive and Super Long Chain (+)-Biotin derivative.
● Extended chain increases avidin binding.¹

1.  Hofman, K., et.al. (1982) Biochemistry 21, 978-984.

Storage 0-4 °C.

● Glycoprotein reactive and Super Long Chain (+)-Biotin derivative.
● Labeling leukocyte surface proteins.¹
● Biotinylating lipopolysaccharides.²
● Used to biotinylate hyaluronan.³

1.  Kahne, T., et.al. (1994) J. Immunol. Meth. 168, 209-218.
2.  Luk, J.M., et.al. (1995) Anal. Biochem. 232, 217-224.
3.  Yu, Q., et.al. (1995) Biotechniques 19(1), 122-129.

Storage 0-4 °C.

● Amino reactive and extended (+)-Biotin.^1,2
● 30.5 Å spacer reduces steric hindrance when binding avidin or streptavidin.
● Solubility:  DMF: 25 mg/mL.

1.  Boado, R.J., Pardridge, W.M. (1992) Bioconjugate Chem. 3, 519.
2.  Hyman, A., et. al. (1991) Meth. Enzymol. 196, 478-485.

Storage 0-4 °C.

● Water soluble!
● Fourteen atom spacer improves avidin binding to labeled substrates.¹

1.  Marmorstein, A.D., et. al. (1998) Cell Biol. 2nd ed. 4, 341.

Storage 0-4 °C.

Storage 0-4 °C.

Storage 0-4 °C.

● Amino-PEO tether imparts water solubility  to this Biotin.
● Extended chain length (20.4 Å) increases avidin binding.¹
● Conjugation to substrates increases the aqueous solubility of the complex.
● Used in affinity purification of oligonucleotides.²

1.  Hofman, K., et.al. (1982) Biochemistry 21, 978-984.
2.  Fang, S.; Bergstrom, D.E. (2003) Bioconjugate Chem. 14, 80-85.

Storage 0-4 °C.

● Amino-PEO tether imparts water solubility  to this Biotin.
● Extended chain length (22.9 Å) reduces steric hindrance and increases avidin binding.¹
● Biotinylation of carbohydrates or glycoproteins.  Conjugation to substrates increases the aqueous solubility of the complex.

1. Hofman, K., et.al. (1982) Biochemistry 21, 978-984.

Storage 0-4 °C.

● Amino-(+)-Biotin derivative for labeling carbohydrates or glycoproteins.¹

1.  Jron, W.M., et.al. (1989) Anal. Biochem. 182, 170.

Storage 0-4 °C.

● Short chain amino biotin.
● Useful for intracellular labeling studies.¹

1.  Kita, H., Armstrong, W. (1991) J. Neurol. Sci. 37, 141.

Storage 0-4 °C.

● (+)-Biotin derivative for crosslinking avidin molecules.
● Wide application in diagnostics.
● Water soluble!
● 43.4 Å PEO spacer.

Storage 0-4 °C.

● (+)-Biotin dimer crosslinks avidin molecules.   Generates linear avidin oligomers.¹
● Useful in immunodiagnostics as a signal enhancer.

1.  Sutoh, K., et.al. (1984) J. Mol. Biol. 178, 323-339.

Storage 0-4 °C.

● (+)-Biotin-fluorescein conjugate for diagnostic applications.
● UV abs l_max 492 nm, e=76,600 M^-1 cm^-1.¹
● PEO tether provides improved water solubility!

1.  Rinderknecht, H. (1962) Nature 193, 167.

Storage 0-4 °C.

(+)-Biotin-(PEO)₄-psoralen; 99 %
C₃₃H₄₄N₄SO₁₀;  M_r=688.79; mp 98-100  °C
Spacer Arm length:  36.9 Å.

● DNA/RNA probe modification does not interfere with hybridization.¹
● Labeling occurs by photolysis at 350 nm, 10-30 min.²
● Psoralen moiety reacts through cycloaddition to the 5,6 double bond in thymine and other pyrimidine containing bases.³
● Water soluble!
● Psoralen functional group is non-hydrolytic.

1.  Henriksen, U., et.al. (1991) Photochem. Photobiol. A: Chem. 57, 331-342.
2.  Wassarman, D.A.  (1993) Molec. Biol. Reports 17, 143-151.
3.  Oser, A., et.al. (1988) Nucleic Acids Res. 16, 1181-1196.

Storage 0-4 °C.

● Water soluble! 
● Labeling occurs by photolysis at 320-350 l.

Storage 0-4 °C.

● Water soluble! 
● Labeling occurs by photolysis at 320 l.
● Tetrafluorophenyl stabilized nitrene gives higher yields of substrate-insertion products.¹

1.  Keana J. F. W., Cai, S. X. (1990) J. Org. Chem. 55, 3640-3647.

Storage 0-4 °C.

● Water soluble!   Sulfhydryl reactive!
● Labels sulfhydryl groups of proteins in aqueous media, i.e. PBS, pH 7.2/ 25 °C.
● Long chain length (24.7 Å)!

Storage 0-4 °C.

● Water soluble!
● Long chain length (29.1 Å)!

Storage 0-4 °C.

● Water soluble!   Sulfhydryl reactive!
● Long chain length!

Storage 0-4 °C.

● Water soluble!  In-situ biotinylation of proteins using EDC·HCl.
● Long chain length (37.5 Å)!  PEO tether inhibits conjugate precipitation.
● N-terminal biotinylation of peptides.
● Biotinylation of oligonucleotides.

Storage 0-4 °C.

● Water soluble!
● Long chain length (38 Å)!
● Biotinylation of glycoproteins.

Storage 0-4 °C.

● Amino reactive and water soluble!
● Long chain length (37.5  Å)!

Storage 0-4 °C.

● Amino reactive and cleavable biotinylation reagent.^1-4
● 24.3 Å chain length.

1.  Cleavable with DTT, DTE, or TCEP.²
2.  Han, J.C., et.al. (1994) Anal. Biochem. 220, 5-10.1.
3.  Moulton, C.A., et. al. (1982) Arch. Biochem. Biophys. 218, 101-108.
4.  Lomant, A.J., Fairbanks, G. (1976) J. Mol. Biol. 104, 243-261.

Storage 0-4 °C.

● Amino-biotin with cleavable tether.
● C-terminal biotinylation of peptides.
● Cleavable with DTT, DTE, or TCEP.¹

1.  Han, J.C., et.al. (1994) Anal. Biochem. 220, 5-10.

Storage 0-4 °C.