Mouse IgG2b Isotype Control (Clone MPC-11-D265A) – Recombinant In vivo Purified No Carrier Protein

Unknown

This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

This recombinant isotype control antibody features the variable regions of clone MPC-11 coupled to an engineered Mouse IgG2b Fc domain containing a D265A mutation to eliminate Fcγ receptor and complement binding. Recombinant antibodies are manufactured in our animal free facility located in St. Louis, Missouri USA using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.

To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s recombinant biosimilar antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.

The Clone MPC-11 recombinant antibody serves as a highly dependable mouse IgG2b negative control for a wide array of immunological assays. Derived from a mouse plasmacytoma, the variable regions of the MPC-11 clone exhibit no specific binding affinity for mammalian target proteins. Because it lacks functional reactivity to human, mouse, or rat tissues, it is the ideal tool for establishing baseline measurements and distinguishing true antigen-specific signals from background noise in flow cytometry, multiplex assays, and functional studies.

Targeted D265A Fc Engineering

To prevent unwanted interactions with cellular receptors, this specific variant of Clone MPC-11 has been engineered with a D265A point mutation (aspartic acid to alanine substitution at position 265) within the IgG2b Fc domain.

Effector Function Silencing: This targeted modification dramatically reduces binding affinity to Fcγ receptors (FcγRI, FcγRII, and FcγRIII) and inhibits C1q complement binding.

Assay Clarity: By effectively mitigating Fc-mediated effector functions and non-specific background binding, the D265A mutation ensures a completely inert profile, making it safe and reliable for sensitive in vitro cultures and in vivo animal models.

1.) Source/Vendor: Sigma-Aldrich / ECACC Catalog Number: 91031103 (or CB_91031103)