Exbio — Research products — Antibodies — MHC antigens — Anti-HLA-DR1 (empty) PE

Anti-HLA-DR1 (empty) PE

Regulatory status

RUO

Antigen

HLA-DR1 (empty)

Clone

MEM-267

Format

Reactivity

Human

Application

FC (QC tested)

Excitation laser

blue (488 nm)

Variant

0.1 mg

1P-435-C100

In stock

286.00 USD

0.025 mg

1P-435-C025

Delivery 1 week

143.00 USD

Variant

0.1 mg

1P-435-C100

In stock

286.00 USD

0.025 mg

1P-435-C025

Delivery 1 week

143.00 USD

Contact distributor

Product details

Description

Images

References

SDS download

Isotype

Mouse IgG2b

Specificity

The antibody MEM-267 specifically binds extracellularly to the empty but not peptide-loaded form of HLA-DR1. DR is the isotypes of human MHC Class II molecules expressed on antigen-presenting cells (APC; dendritic cells, B lymphocytes, monocytes, macrophages).

Application

FC (QC tested)

Application details

Flow cytometry: The antibody MEM-267 stains immature dendritic cells that express empty cell surface MHC molecules, but not cells that express predominantly peptide loaded forms. Recommended dilution: 1-5 μg/ml.

Reactivity

Human

Immunogen

Purified, insoluble DR1 beta chain (DRB1*0101) expressed in E. coli inclusion bodies.

Concentration

0.1 mg/ml

Preparation

Purified antibody is conjugated with R-phycoerythrin (PE) under optimum conditions. Unconjugated antibody and free fluorochrome are removed by size-exclusion chromatography.

Formulation

Stabilizing phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

Storage and handling

Store at 2-8°C. Protect from prolonged exposure to light. Do not freeze.

The product is intended For Research Use Only. Diagnostic or therapeutic applications are strictly forbidden. Products shall not be used for resale or transfer to third parties either as a stand-alone product or as a manufacture component of another product without written consent of EXBIO Praha, a.s. EXBIO Praha, a.s. will not be held responsible for patent infringement or any other violations of intellectual property rights that may occur with the use of the products. Orders for all products are accepted subject to the Term and Conditions available at www.exbio.cz. EXBIO, EXBIO Logo, and all other trademarks are property of EXBIO Praha, a.s.

Antigen description

HLA-DR1 belongs to the HLA class II beta chain paralogues. The MHC Class II molecule is a heterodimer consisting of an alpha (DRA) and a beta chain (DRB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. MHC Class II molecules are expressed in antigen presenting cells (APC). The beta chain is approximately 26-28 kDa. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Hundreds of DRB1 alleles have been described and typing for these polymorphisms is routinely done for bone marrow and kidney transplantation.

Flow cytometry surface staining pattern of human peripheral whole blood stained using anti-human HLA-DR1-empty (MEM-267) PE antibody (concentration in sample 9 μg/ml).

Flow cytometry multicolor surface staining pattern of human peripheral whole blood stained using anti-human HLA-DR1-empty (MEM-267) PE antibody (concentration in sample 9 μg/ml) and anti-human HLA-DR (L243) APC antibody (10 μl reagent / 100 μl of peripheral whole blood).

Separation of human HLA-DR1 (empty) positive HLA-DR positive cells (red-filled) from neutrophil granulocytes (black-dashed) in flow cytometry analysis (surface staining) of human peripheral whole blood stained using anti-human HLA-DR1-empty (MEM-267) PE antibody (concentration in sample 9 μg/ml).

Product specific references:

Potolicchio I, Chitta S, Xu X, Fonseca D, Crisi G, Horejsi V, Strominger JL, Stern LJ, Raposo G, Santambrogio L: Conformational variation of surface class II MHC proteins during myeloid dendritic cell differentiation accompanies structural changes in lysosomal MIIC. J Immunol. 2005 Oct 15;175(8):4935-47.
PubMed

Carven GJ, Chitta S, Hilgert I, Rushe MM, Baggio RF, Palmer M, Arenas JE, Strominger JL, Horejsi V, Santambrogio L, Stern LJ: Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding. J Biol Chem. 2004 Apr 16;279(16):16561-70.
PubMed