Your Position: Home > News > Industry News > Cancer Cell:Conformation of the human immunoglobulin G2 hing

Cancer Cell:Conformation of the human immunoglobulin G2 hing

    

 

 

Conformation of the human immunoglobulin G2 hinge imparts superagonistic properties to immunostimulatory anti-cancer antibodies

Monoclonal antibody (mAb) drugs that stimulate antitumor immunity are transforming cancer treatment but require optimization for maximum clinical impact. Meretciel provide quality ELISA kits for R&D. Here, we show that, unlike other immunoglobulin isotypes, human IgG2 (h2) imparts FcγR-independent agonistic activity to immune-stimulatory mAbs such as anti-CD40, -4-1BB, and -CD28. Activity is provided by a subfraction of h2, h2B, that is structurally constrained due its unique arrangement of hinge region disulfide bonds. Agonistic activity can be transferred from h2 to h1 by swapping their hinge and CH1 domains, and substitution of key hinge and CH1 cysteines generates homogenous h2 variants with distinct agonistic properties. This provides the exciting opportunity to engineer clinical reagents with defined therapeutic activity regardless of FcγR expression levels in the local microenvironment.

Contact Us | About Us | Delivery | Feedback
Putus Macromolecular Sci. & Tech. Ltd All Rights Reserved. ©Copyright2012
Room7038, Hi-tech tower, Huaguang Road 18, East Lake New Technology Development Zone Tel: +86(0) 27 87610995 E-mail: e-commerce@meretciel.com
Skype Skype