Against the backdrop of the rapid development of antibody and ADC drugs, the accurate detection of Human IgG mutants has become a key challenge in drug development. Based on advanced nanobody (VHH) technology, AlpVHHs has launched the innovative Anti-Human IgG (CH2 Fragment Specific) AlpSdAbs® VHH series, which can accurately identify various IgG engineered mutants, providing a reliable tool for antibody activity detection and quality control.
The CH2 domain is the core functional unit of the Human IgG Fc region, directly mediating binding to the Fcγ receptor (FcγR) and complement protein C1q. It is an important structural basis for regulating various immune effects, including:
● ADCC (Antibody-dependent Cell-Mediated Cytotoxicity)
● CDC (Complement-Dependent Cytotoxicity)
Therefore, the CH2 domain plays a crucial role in antibody drug design and functional regulation.
In recent years, antibody engineering technology has become a core pathway for upgrading ADC drugs. Common mutations include:
● LALA mutation: Reduces FcγR binding ability, avoids immune cell-mediated non-specific killing, and improves tumor targeting specificity.
● YTE mutation: Improves FcRn binding ability and significantly prolongs antibody half-life.
● KIH (Knob-into-Hole) mutation: Used to construct bispecific antibodies and solve heavy chain mismatch problems.
However, these key mutations are concentrated in the CH2-CH3 region, which directly alters the recognition epitopes of traditional antibodies, leading to:
● Failure of conventional Anti-Human IgG secondary antibody recognition
● Unstable detection signals in ELISA/WB/Flow assays
● Difficulty in evaluating antibody activity
To address industry challenges, Critical Point Biotech has developed the Anti-Human IgG (CH2 Fragment Specific) AlpSdAbs® VHH series of nanoantibodies. Based on a single-domain nanobody (VHH) platform, this product can simultaneously and accurately identify:
● Wild Type Human IgG
● LALA mutants
● LALA + YTE combined mutants
● KIH bispecific antibody structures
Providing a more stable and reliable detection tool for antibody drug development, ADC detection, and bispecific antibody analysis.
Anti-Human IgG (CH2 Fragment Specific) nano-secondary antibody specifically binds to the CH2 domain of Human IgG and:
● Does not cross-react with other IgG domains
● Significantly improves detection specificity and accuracy
● More accurately reflects the structural characteristics of antibody drugs
Suitable for applications such as Human IgG detection, ADC detection, and antibody structure analysis.
Traditional secondary antibodies often suffer from non-specific binding to the Fc receptor due to their Fc structure. VHH nanobodies, however:
● Contain no Fc fragments
● Fundamentally eliminate Fc-mediated non-specific binding
● Significantly reduce background signal
Especially suitable for Flow Cytometry, Immunohistochemistry (IHC), and Immunofluorescence to obtain clearer detection results.
This product utilizes recombinant monoclonal nanobody expression technology, ensuring a fully controllable production process. Advantages include:
● Minimal batch variation
● Stable affinity (Kd)
● Highly consistent specificity
● Excellent reproducibility of experimental results
Fully meets the stringent requirements for antibody drug development and quality control.
The product offers a variety of commonly used labeling formats, including: HRP, Biotin, PE, APC, iFluor488, iFluor594, and iFluor647; widely applicable to: ELISA, Western Blot (WB), Flow Cytometry, Immunocytochemistry / Immunofluorescence (ICC / IF), and Immunoprecipitation (IP).
(1) Validation Data for Different Mutant Antibodies
ELISA results showed that Anti-Human IgG (CH2 Fragment specific), AlpSdAbs® VHH(HRP) (Code: 023-112-005) can simultaneously identify multiple Human IgG1 mutants, including WT, LALA, LALA+YTE, and KIH.
(2) Validation Data For Different Subtypes Antibodies
ELISA results showed that Anti-Human IgG (CH2 Fragment specific), AlpSdAbs® VHH(HRP) (Code: 023-112-005) exhibited high sensitivity in binding to and specific recognition of the Human IgG CH2 fragment for all Human IgG subtypes 1/2/4.
With the rapid development of ADCs, bispecific antibodies, and engineered antibodies, traditional antibody detection tools are no longer sufficient to meet the demands. AlpVHHs' recombinant nano-secondary antibody, through its precise design philosophy, industrialized production standards, and unique molecular morphology, systematically addresses the pain points of traditional polyclonal antibodies. It is not only a superior detection reagent but also a key enabling tool for improving the quality, reproducibility, and efficiency of antibody drug development data, providing a solid foundation for the rapid and robust development of innovative drugs.
Code | Description | Application |
023-112-010 | Flow Cyt | |
023-112-011 | Flow Cyt | |
023-112-004 | Anti-Human IgG(CH2 Fragment specific), AlpSdAbs® VHH(Biotin) | WB,ELISA,IP |
023-112-005 | WB,ELISA | |
023-112-007 | Anti-Human IgG(CH2 Fragment specific), AlpSdAbs® VHH(iFluor488 ×4) | WB,ELISA,ICC/IF,Flow Cyt |
023-112-008 | Anti-Human IgG(CH2 Fragment specific), AlpSdAbs® VHH(iFluor594 ×4) | WB,ELISA,ICC/IF,Flow Cyt |
023-112-009 | Anti-Human IgG(CH2 Fragment specific), AlpSdAbs® VHH(iFluor647 ×4) | WB,ELISA,ICC/IF,Flow Cyt |
023-312-001 | Anti-Human IgG(CH2 Fragment specific), AlpHcAbs® Mouse antibody | ICC/IF,Flow Cyt,IP,WB,ELISA |
023-312-004 | Anti-Human IgG(CH2 Fragment specific), AlpHcAbs® Mouse antibody(Biotin) | WB,ELISA,IP |
023-312-005 | Anti-Human IgG(CH2 Fragment specific), AlpHcAbs® Mouse antibody(HRP) | WB,ELISA |
