About Carboxypeptidase B2
Carboxypeptidases are enzymes that hydrolyze C-terminal peptide bonds. The carboxypeptidase family includes metallo-, serine, and cysteine carboxypeptidases. According to their substrate specificity, these enzymes are referred to as carboxypeptidase A (cleaving aliphatic residues) or carboxypeptidase B (cleaving basic amino residues). The protein encoded by this gene is activated by trypsin and acts on carboxypeptidase B substrates. After thrombin activation, the mature protein downregulates fibrinolysis. Polymorphisms have been described for this gene and its promoter region. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jun 2013]

About DyLight 550
DyLight™ 550 has an excitation peak at 562 nm and an emission peak at 576 nm and is spectrally similar to Alexa Fluor™ 546, Alexa Fluor™ 555, Cy3 and TRITC. DyLight™ 550 is most commonly used in flow cytometery and fluorescence microscopy applications.