Products
Monalizumab Biosimilar Monoclonal Antibody (NKG2A) for Research
Pre-Made Monalizumab biosimilar, Whole mAb, Anti-KLRC1/NKG2A Antibody: Anti-CD159A/NKG2 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.
Monalizumab (formerly IPH2201) is an investigational drug being studied for rheumatoid arthritis, gynecologic malignancies and other cancers.
Order Information
| Catalog No. | Package | List Price(In USD) | Discount off | Discount Price |
|---|---|---|---|---|
| GMP-Bios-ab-355-1mg | 1mg | 3090 |
Size： 1mg | 10mg | 100mg
Product Details
| Products Name (INN Index) | Pre-Made Monalizumab biosimilar, Whole mAb, Anti-KLRC1/NKG2A Antibody: Anti-CD159A/NKG2 therapeutic antibody |
| INN Name | Monalizumab |
| Target | NKG2A |
| Format | Whole mAb |
| Derivation | Humanized |
| Species Reactivity | Human |
| CH1 Isotype | IgG4 |
| VD LC | Kappa |
| Highest_Clin_Trial (Jan '20) | Phase-III |
| Est. Status | Active |
| 100% SI Structure | None |
| 99% SI Structure | None |
| 95-98% SI Structure | None |
| Year Proposed | 2015 |
| Year Recommended | 2016 |
| Companies | Innate Pharma;MedImmune;NCIC Clinical Trials Group;Novo Nordisk |
| Conditions Approved | na |
| Conditions Active | Head and neck cancer;Non-small cell lung cancer;Cervical cancer;Chronic lymphocytic leukaemia;Endometrial cancer;Fallopian tube cancer;Ovarian cancer;Peritoneal cancer;Solid tumours;Haematological malignancies |
| Conditions Discontinued | Inflammation;Rheumatoid arthritis |
| Development Tech | na |
About target - KLRC1
1. Protein NKG2-A/NKG2-B type II integral membrane protein
2. Gene KLRC1
3. Organism Homo sapiens (Human)
Function
Immune inhibitory receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self (PubMed:9486650, PubMed:18083576, PubMed:9430220).
Upon HLA-E-peptide binding, transmits intracellular signals through two immunoreceptor tyrosine-based inhibition motifs (ITIMs) by recruiting INPP5D/SHP-1 and INPPL1/SHP-2 tyrosine phosphatases to ITIMs, and ultimately opposing signals transmitted by activating receptors through dephosphorylation of proximal signaling molecules (PubMed:9485206, PubMed:12165520).
Key inhibitory receptor on natural killer (NK) cells that regulates their activation and effector functions (PubMed:9486650, PubMed:9430220, PubMed:9485206, PubMed:30860984).
Dominantly counteracts T cell receptor signaling on a subset of memory/effector CD8-positive T cells as part of an antigen-driven response to avoid autoimmunity (PubMed:12387742).
On intraepithelial CD8-positive gamma-delta regulatory T cells triggers TGFB1 secretion, which in turn limits the cytotoxic programming of intraepithelial CD8-positive alpha-beta T cells, distinguishing harmless from pathogenic antigens (PubMed:18064301).
In HLA-E-rich tumor microenvironment, acts as an immune inhibitory checkpoint and may contribute to progressive loss of effector functions of NK cells and tumor-specific T cells, a state known as cell exhaustion (PubMed:30503213, PubMed:30860984).
(Microbial infection) Viruses like human cytomegalovirus have evolved an escape mechanism whereby virus-induced down-regulation of host MHC class I molecules is coupled to the binding of viral peptides to HLA-E, restoring HLA-E expression and inducing HLA-E-dependent NK cell immune tolerance to infected cells. Recognizes HLA-E in complex with human cytomegalovirus UL40-derived peptide (VMAPRTLIL) and inhibits NK cell cytotoxicity.
(Microbial infection) May recognize HLA-E in complex with HIV-1 gag/Capsid protein p24-derived peptide (AISPRTLNA) on infected cells and may inhibit NK cell cytotoxicity, a mechanism that allows HIV-1 to escape immune recognition.
(Microbial infection) Upon SARS-CoV-2 infection, may contribute to functional exhaustion of cytotoxic NK cells and CD8-positive T cells (PubMed:32203188, PubMed:32859121).
On NK cells, may recognize HLA-E in complex with SARS-CoV-2 S/Spike protein S1-derived peptide (LQPRTFLL) expressed on the surface of lung epithelial cells, inducing NK cell exhaustion and dampening antiviral immune surveillance (PubMed:32859121).
