Anti-Human HLA-DR (MHC Class II) – Purified in vivo PLATINUM™ Functional Grade
Pricing & Details
≥ 5.0 mg/ml
<0.5 EU/mg as determined by the LAL method
≥98% monomer by analytical SEC
>95% by SDS Page
This monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added.
Functional grade preclinical antibodies are manufactured in an animal free facility using only In vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s Purified Functional PLATINUMTM antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile.
Storage and Handling
Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at -80°C. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
Next Day 2-8°C
Applications and Recommended Usage?
Quality Tested by Leinco
FC The suggested concentration for this HLA-DR (Clone L243) antibody for staining cells in flow cytometry is ≤ 0.5 μg per 106 cells in a volume of 100 μl or 100μl of whole blood. Titration of the reagent is recommended for optimal performance for each application.
WB The suggested concentration for this HLA-DR (Clone L243) antibody for use in western blotting is 1-10 μg/ml.
Other Applications Reported In Literature ?
Additional Reported Applications For Relevant Conjugates ?
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.
Clone L243 recognizes a conformational epitope on the human MHC class II molecule HLA-DRα, which depends on the correct folding of the αβ heterodimer1. It does not cross-react with HLA-DP or HLA-DQ.
HLA-DR is expressed on antigen-presenting cells, including macrophages, monocytes, DCs, and B cells, and activated T cells.
HLA-DR antibody, clone L243, recognizes the major histocompatibility complex (MHC) class II molecule Human Leukocyte Antigen - DR isotype (HLA-DR). MHC class II is constitutively expressed on human professional antigen-presenting cells (APCs), including macrophages/monocytes, dendritic cells (DCs), and B cells, and is induced on T cells upon activation2. HLA-DR consists of two transmembrane proteins, a 35 kDa α (heavy) chain and 29 kDa β (light) chain3 encoded by the HLA-DRA and HLA-DRB1, HLA-DRB3, HLA-DRB4, and HLA-DRB5 genes, respectively, located in the HLA complex of chromosome 6. The N-terminal α1 and β1 domains form the antigen-binding groove, which binds 13-25 aa peptides derived from exogenous antigens4. On APCs, MHC class II plays a critical role in the adaptive immune response by presenting phagocytosed antigens to helper CD4 T cells. The T cell receptor (TCR)/CD3 complex of CD4 T cells interacts with peptide-MHC class II, which induces CD4 T cell activation leading to the coordination and regulation of other effector cells. CD4 molecules also bind to MHC class II, which helps augment TCR signaling5. It has also been demonstrated that MHC class II express on activated T cells are capable of antigen presentation6 and can transduce signals into T cells, enhancing T cell proliferation and activity7. HLA-DR expression is a marker of T cell activation and correlates with disease activity in patients with autoimmune disease8 and rapid progression in HIV infection9. Specific alleles of HLA-DR are associated with autoimmune diseases, including rheumatoid arthritis10.
NCBI Gene Bank ID
References & Citations
1. Moro M, Cecconi V, Martinoli C, et al. (2005) BMC Immunol. 6:24
2. Holling TM, et al. (2004) Hum Immunol. 65(4):282-90
3. Mitaksov V, (2006) J Biol Chem. 281(15):10618-25
4. Wieczorek M, et al. (2017) Front Immunol. 8:292
5. Artyomov MN, et al. (2010) Proc Natl Acad Sci USA. 107(39):16916-16921
6. Barnaba V, et al. (1994) Eur J Immunol. 24(1):71-5
7. Di Rosa F, et al. (1993) Hum Immunol. 38(4):251-60
8. Viallard JF, et al. (2001) Clin Exp Immunol. 125(3):485-491
9. Langford SE, Ananworanich J, Cooper DA. (2007) AIDS Res Ther. 2007;4:11
10. Gough SC, Simmonds MJ. (2007) Curr Genomics. 8(7):453-465