B2M Antibodies
Background
β2 microglobulin encoded by the B2M gene is a small globular protein that is widely present on the surface of nucleated cells and serves as a light chain component of the major histocompatibility complex (MHC-class I molecules). This protein participates in the antigen presentation process by non-covalently binding to heavy chains and plays a key role in immune recognition and regulation. Mutations or abnormal expression of the B2M gene are associated with a variety of diseases, including autoimmune diseases, malignant tumors and renal failure, etc. This gene was first isolated and identified by Berggard et al. in 1973. Its three-dimensional structure was analyzed by X-ray crystallography, providing an important foundation for understanding the interaction of immune molecules and the development of drug targets. The stability and conservation of B2M protein make it one of the classic models for studying protein folding and disease mechanisms.
Structure of B2M
B2M is a protein with a relatively small molecular weight, approximately 11.8 kDa. This value may vary slightly among different species, mainly due to minor changes in amino acid sequences.
Species | Human | Mouse | Rat | Bovine |
Molecular Weight (kDa) | 11.8 | 11.9 | 11.8 | 11.7 |
Primary Structural Differences | Conserved sequence, highly homologous to most mammals | Amino acid substitution at individual sites | There are subtle differences from rats and mice | High similarity to the human sequence |
The B2M protein is composed of 119 amino acids, and its primary structure forms a typical immunoglobulin folding domain, presenting a compact spherical shape. This protein does not contain a cofactor, but its folding conformation depends on a conserved disulfide bond (linking cysteine at positions 25 and 80), which is crucial for maintaining its structural stability. The secondary structure of B2M is mainly composed of β -sheets. These anti-parallel β -folded chains form two β -sheet structures, which are tightly connected by disulfide bonds and jointly form a hydrophobic core, which is the key structural basis for its combination with MHC class I molecular heavy chains.
Fig. 1 The association of B2M with immunotherapy resistance and reversal strategies.1
Key structural properties of B2M:
- Typical immunoglobulin fold structure (Ig-fold)
- Conservative disulfide bond (Cys25 - Cys80) stable overall 3d structure
- Folding conformation directly mediated the MHC class I molecules heavy chain interaction
Functions of B2M
The main function of B2M is to serve as an essential light chain for the major histocompatibility complex (MHC Class I molecules) and participate in the antigen presentation process. In addition, it also involves a variety of pathophysiological processes, including immune regulation and the role of disease markers.
Function | Description |
Antigen presentation | B2M non-covalently binds to MHC Class I heavy chains, stabilizes their structure and presents endogenous antigenic peptides to CD8⁺T cells, triggering specific immune responses. |
Immune recognition | As a component of MHC I molecules, it directly participates in the process of T cells' recognition and clearance of infected cells or tumor cells. |
Assessment of renal function | The concentration of free B2M in the blood is a sensitive biomarker for evaluating glomerular filtration function, and its increase indicates impaired renal function. |
Markers of disease status | In some autoimmune diseases (such as rheumatoid arthritis) and hematological malignancies (such as multiple myeloma), its level is abnormally elevated. |
Cell surface stability is maintained | By binding with MHC I heavy chains, it helps maintain the correct expression and stability on the cell membrane surface and prevent degradation. |
The B2M molecule itself does not have polymorphism. Its binding to polymorphic heavy chains is the structural basis for MHC Class I molecules to achieve a wide range of antigen presentation functions. This characteristic makes it a key bridge molecule in the adaptive immune system.
Applications of B2M and B2M Antibody in Literature
1. Zhang, Hao, et al. "B2M overexpression correlates with malignancy and immune signatures in human gliomas." Scientific Reports 11.1 (2021): 5045. https://doi.org/10.1038/s41598-021-84465-6
The article indicates that based on the analysis of TCGA and CGGA data, it is found that high expression of B2M is associated with a poor prognosis of glioma, and is significantly related to PTEN deficiency, EGFR amplification and immune infiltration. B2M inhibits anti-tumor immunity by regulating immune checkpoint molecules and inflammatory activity, and it is a potential target for immunotherapy.
2. Ravindranath, Mepur H., et al. "Cell surface B2m-free human leukocyte antigen (Hla) monomers and dimers: are they neo-hla class and proto-hla?." Biomolecules 13.8 (2023): 1178. https://doi.org/10.3390/biom13081178
The article indicates that there are HLA-I heavy chain monomers (Face-2) independent of B2m and their homologous/heterodimers (Face-3/4) on the cell surface. When B2m is absent, Face-2 is upregulated in normal tissues and cancer cells, associated with inflammation and autoimmunity, and may be involved in immune regulation through interactions with multiple ligands.
3. Han, aowen, et al. "The role of B2M in cancer immunotherapy resistance: function, resistance mechanism, and reversal strategies." Frontiers in Immunology 16 (2025): 1512509. https://doi.org/10.3389/fimmu.2025.1512509
The article indicates that B2M is an MHC-I light chain and plays a key role in the presentation of tumor antigens. Its mutations or defects can lead to drug resistance in tumor immunotherapy, becoming the main obstacle limiting the therapeutic effect. Clarifying the role of B2M and developing countermeasures against it is currently an important direction for improving the efficacy of immunotherapy.
4. Hu, Mingxin, et al. "B2M or CIITA knockdown decreased the alloimmune response of dental pulp stem cells: an in vitro study." Stem Cell Research & Therapy 15.1 (2024): 425. https://doi.org/10.1186/s13287-024-04023-5
The article indicates that by knocking down B2M or CIITA, the HLA-I/II expression of DPSCs is decreased, the immunogenicity is significantly weakened, and the characteristics of stem cells are not affected, providing a new strategy for expanding its clinical application.
5. Lin, Hailian, et al. "[Retracted] Analysis of the B2M Expression in Colon Adenocarcinoma and Its Correlation with Patient Prognosis." Evidence‐Based Complementary and Alternative Medicine 2022.1 (2022): 7264503. https://doi.org/10.1155/2022/7264503
Research has found that the expression of B2M is decreased in colonic adenocarcinoma. The reduction in its expression after mutation may lead to tumor immune escape, affecting treatment outcomes and prognosis, suggesting that B2M may serve as a potential tumor suppressor gene for COAD.
Creative Biolabs: B2M Antibodies for Research
Creative Biolabs specializes in the production of high-quality B2M antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.
- Custom B2M Antibody Development: Tailor-made solutions to meet specific research requirements.
- Bulk Production: Large-scale antibody manufacturing for industry partners.
- Technical Support: Expert consultation for protocol optimization and troubleshooting.
- Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.
For more details on our B2M antibodies, custom preparations, or technical support, contact us at email.
Reference
- Han, aowen, et al. "The role of B2M in cancer immunotherapy resistance: function, resistance mechanism, and reversal strategies." Frontiers in Immunology 16 (2025): 1512509. https://doi.org/10.3389/fimmu.2025.1512509
Anti-B2M antibodies

Hot products 
- AActivation
- AGAgonist
- APApoptosis
- BBlocking
- BABioassay
- BIBioimaging
- CImmunohistochemistry-Frozen Sections
- CIChromatin Immunoprecipitation
- CTCytotoxicity
- CSCostimulation
- DDepletion
- DBDot Blot
- EELISA
- ECELISA(Cap)
- EDELISA(Det)
- ESELISpot
- EMElectron Microscopy
- FFlow Cytometry
- FNFunction Assay
- GSGel Supershift
- IInhibition
- IAEnzyme Immunoassay
- ICImmunocytochemistry
- IDImmunodiffusion
- IEImmunoelectrophoresis
- IFImmunofluorescence
- IHImmunohistochemistry
- IMImmunomicroscopy
- IOImmunoassay
- IPImmunoprecipitation
- ISIntracellular Staining for Flow Cytometry
- LALuminex Assay
- LFLateral Flow Immunoassay
- MMicroarray
- MCMass Cytometry/CyTOF
- MDMeDIP
- MSElectrophoretic Mobility Shift Assay
- NNeutralization
- PImmunohistologyp-Paraffin Sections
- PAPeptide Array
- PEPeptide ELISA
- PLProximity Ligation Assay
- RRadioimmunoassay
- SStimulation
- SESandwich ELISA
- SHIn situ hybridization
- TCTissue Culture
- WBWestern Blot
