M7398
Monoclonal Anti-β2-Microglobulin antibody produced in mouse
clone BM-63, ascites fluid
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About This Item
Produits recommandés
Source biologique
mouse
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
ascites fluid
Type de produit anticorps
primary antibodies
Clone
BM-63, monoclonal
Poids mol.
antigen 12 kDa
Contient
15 mM sodium azide
Espèces réactives
human
Technique(s)
indirect ELISA: 1:1000
indirect immunofluorescence: 1:500 using human PBL′s
Isotype
IgG1
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... B2M(567)
Description générale
β-2-microglobulin is part of the human leukocyte antigen, where it represents the light chain. It is expressed on cell membranes and is made up of 99 amino acids. β-2-microglobulin is part of the immunoglobulin superfamily. β−2-Microglobulin is a membrane glycoprotein of mammalian nucleated cells including lymphocytes.
Monoclonal anti-β-2-Microglobulin (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse.
Immunogène
human β2-microglobulin and a lysate of a lymphoblastoid cell line.
Application
Monoclonal Anti-β2-Microglobulin antibody produced in mouse has been used in ELISA and immunofluorescent labelling.
Actions biochimiques/physiologiques
β-2-microglobulin acts as a tumor marker and has been shown to be associated with dialysis-related amyloidosis. It may function as a structural part of the MHC Class I molecule.
Microglobulin may be elevated in the serum or urine of patients with systemic lupus erythematosus (SLE), rheumatoid arthritis, metal toxications, some viral infections and possibly malignant disorders and AIDS.
Clause de non-responsabilité
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
nwg
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Serum Beta 2-microglobulin/cystatin C index: a useful biomarker in lupus nephritis
Silva MVM, et al.
Nephron extra, 2(1), 169-176 (2012)
Alon Margalit et al.
Journal of immunology (Baltimore, Md. : 1950), 176(1), 217-224 (2005-12-21)
Level and persistence of antigenic peptides presented by APCs on MHC class I (MHC-I) molecules influence the magnitude and quality of the ensuing CTL response. We recently demonstrated the unique immunological properties conferred on APCs by expressing beta2-microglobulin (beta2m) as
The production, purification and crystallization of a soluble form of the nonclassical MHC HLA-G: the essential role of cobalt
Clements CS, et al.
Acta Crystallographica Section F, Structural Biology and Crystallization Communications, 62(1), 70-73 (2006)
A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum.
G Diedrich et al.
Journal of immunology (Baltimore, Md. : 1950), 166(3), 1703-1709 (2001-02-13)
Heterodimers of MHC class I glycoprotein and beta(2)-microglobulin (beta(2)m) bind short peptides in the endoplasmic reticulum (ER). Before peptide binding these molecules form part of a multisubunit loading complex that also contains the two subunits of the TAP, the transmembrane
Justin T H Chan et al.
Science advances, 4(11), eaar7653-eaar7653 (2018-11-13)
Memory B cells and plasma cells are antigen-experienced cells tasked with the maintenance of humoral protection. Despite these prominent functions, definitive cell surface markers have not been identified for these cells. We report here the isolation and characterization of the
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