Antibody Modification and
ADC Payloads Development
ADC Analysis and
The most basic immunoglobulin G molecule consists of two light chains and
two heavy chains connected by non-covalent binding forces and disulfide
bonds. The two heavy chains are connected by a disulfide bond in the hinge
region (hinge region). The disulfide bond connecting the two heavy chains in
the hinge region can be specifically cleaved by reducing agents such as MEA,
dithiothreitol (DTT) and tris (2-carboxyethyl) phosphine (TCEP) to generate two
Half-antibody molecules, each containing an antigen-binding site.
A humanized antibody contains 80 to 90 lysins, so modification of partial
lysine has no effect on the natural disulfide bond, nor does it significantly
change the stability, biophysical properties, or affinity of the antibody.
However, through lysine conjugation, each antibody will be coupled with 0~8
small molecule drugs, and the location of the coupling may occur on nearly 40
different lysine residues on the light and heavy chains of the antibody, and
more than 1 million ADCs will be generated.
Antibody-drug Conjugate (ADC) Development
ADCs Cytotoxin with Linkers
BOC Sciences has been committed to providing customers with high-quality products and services for
antibody-drug conjugate research. Our unparalleled platform and outstanding drug discovery expertise
allow us to provide you with comprehensive data and unique insights to provide you with the depth and
breadth of science to advance your drug discovery program.
BOC Sciences offers customers with comprehensive one-stop-shop of all aspects in antibody-drug
conjugate (ADC) research and evaluation, ranging from antibody modification and conjugation
technologies, ADC payloads developm