Biocytin hydrazide

Biocytin hydrazide (0.3-30 μg/mL) optimally labels oxidized fetuin and asialofetuin on dot blots at a concentration of 3 μg/mL^[1].
Biocytin hydrazide (3 μg/mL; 1 h, 2 h) labels human erythrocyte membrane glycoproteins on blots via both periodate oxidation (3 μg/mL, 1 h) and NAGO oxidation (3 μg/mL, 2 h), producing similar banding patterns with NAGO requiring higher protein input^[1].
Biocytin hydrazide (10-100 μg/mL; 1 h, 2 h) labels human erythrocyte membrane glycoproteins via periodate oxidation (10-100 μg/mL, 1 h), NAGO oxidation (10-100 μg/mL, 2 h), or GO oxidation (10-100 μg/mL, 2 h); GO treatment selectively labels the Band 3 glycoprotein, while periodate treatment alters membrane protein electrophoretic mobility^[1].
Biocytin hydrazide achieves site-specific biotinylation of K99 lectin via carboxyl groups. The obtained biotinylated K99 lectin can specifically bind to sialic acid-containing receptors on HeLa cells and recapitulate the adhesion pattern of intact K99-expressing E. coli B80. Meanwhile, biotinylated K99 lectin retains specific recognition capacity toward NeuGc-GM3 ganglioside with a detection limit of 90 ng, showing equivalent sensitivity to intact K99-expressing bacteria^[2].
Biocytin hydrazide (0.01-1 M; 5-96 h) directly biotinylates peptides including human angiotensin I, P₁₄R, ACTH fragment 1-13, and proteins including bovine insulin, horse heart cytochrome c, hen egg white lysozyme, soybean trypsin inhibitor, and bovine serum albumin via its hydrazide moiety, binding to arginine side chains along with other residues, with efficiency increasing with higher temperature, higher concentration, and longer incubation time, and optimal activity at neutral pH^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.