| Host: | Mouse |
| Applications: | ELISA/GICA/CLIA |
| Reactivity: | Human |
| Note: | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO) MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS |
| Short Description : | Mouse monoclonal antibody anti-Beta-2-Microglobulin Cleaved Into-Beta-2-Microglobulin Form Pi 5.3 is suitable for use in ELISA, GImmunocytochemistryA and CLIA research applications. |
| Clonality : | Monoclonal |
| Clone ID : | 1A053 |
| Conjugation: | Unconjugated |
| Isotype: | IgG |
| Formulation: | PBS buffer |
| Purification: | Protein A/G purified from cell culture supernatant |
| Concentration: | 1 mg/mL |
| Storage Instruction: | Suitable for storage at +4°C between 1-2 weeks For longer term store at-20°C for up to 12 months |
| Gene Symbol: | B2M |
| Gene ID: | 567 |
| Uniprot ID: | B2MG_HUMAN |
| Immunogen: | Human Beta-2-microglobulin Protein |
| Function | Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation. |
| Protein Name | Beta-2-Microglobulin Cleaved Into - Beta-2-Microglobulin Form Pi 5.3 |
| Database Links | Reactome: R-HSA-1236974Reactome: R-HSA-1236977Reactome: R-HSA-164940Reactome: R-HSA-198933Reactome: R-HSA-2172127Reactome: R-HSA-2424491Reactome: R-HSA-6798695Reactome: R-HSA-877300Reactome: R-HSA-9637628Reactome: R-HSA-9705671Reactome: R-HSA-977225Reactome: R-HSA-983170 |
| Cellular Localisation | SecretedCell SurfaceDetected In Serum And Urine(Microbial Infection) In The Presence Of MTuberculosis Esxa-Esxb Complex Decreased Amounts Of B2m Are Found On The Cell Surface |
| Alternative Antibody Names | Anti-Beta-2-Microglobulin Cleaved Into - Beta-2-Microglobulin Form Pi 5.3 antibodyAnti-B2M antibodyAnti-CDABP0092 antibodyAnti-HDCMA22P antibody |
Information sourced from Uniprot.org
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