Products
Quilizumab Biosimilar Monoclonal Antibody (IgE) for Research
Pre-Made Quilizumab biosimilar, Whole Mab: Anti-IGHE/IgE therapeutic antibody is a biosimilar expressed by mammalian cell line as a benchmark reference therapeutic antibody for biological drug disovery items including cell culture, assay development, animal model development, PK/PD model development (Pharmacokinetics & Pharmacodynamic) and mechanism of action (MOA) research.
Quilizumab (INN) is a humanized monoclonal antibody designed for the treatment of asthma.[1] It binds to IGHE.
Order Information
| Catalog No. | Package | List Price(In USD) | Discount off | Discount Price |
|---|---|---|---|---|
| GMP-Bios-ab-462-1mg | 1mg | 3090 |
Size： 1mg | 10mg | 100mg
Product Details
| Products Name (INN Index) | Pre-Made Quilizumab biosimilar, Whole Mab: Anti-IGHE/IgE therapeutic antibody |
| INN Name | Quilizumab |
| Target | IGHE |
| Format | Whole mAb |
| Derivation | Humanized |
| Species Reactivity | Human |
| CH1 Isotype | IgG1 |
| VD LC | Kappa |
| Highest_Clin_Trial (Jan '20) | Phase-II |
| Est. Status | Discontinued |
| 100% SI Structure | 3hr5:HL:JQ:BA:IP |
| 99% SI Structure | None |
| 95-98% SI Structure | None |
| Year Proposed | 2011 |
| Year Recommended | 2012 |
| Companies | Genentech |
| Conditions Approved | na |
| Conditions Active | na |
| Conditions Discontinued | Allergic asthma;Allergic rhinitis;Urticaria |
| Development Tech | na |
About target - IGHE
1. Protein Immunoglobulin heavy constant epsilon
2. Gene IGHE
3. Organism Homo sapiens (Human)
Function
Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268).
The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268).
Caution
For an example of a full-length immunoglobulin epsilon heavy chain see AC P0DOX4.
