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Your Position: Home > Protein > HLA-DQA1*03:02 | DQB1*03:03 > HL3-H5285

Human HLA-DQA1*03:02&DQB1*03:03 Monomer Protein (Peptide free)

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  • Source
    Human HLA-DQA1*03:02&DQB1*03:03 Monomer Protein(HL3-H5285) is expressed from human 293 cells (HEK293). It contains AA Glu 24 - Glu 217 (HLA-DQA1*03:02) & Arg 33 - Lys 230 (HLA-DQB1*03:03) (Accession # P01909-1 (HLA-DQA1*03:02) & P01920-1 (HLA-DQB1*03:03)).
  • Molecular Characterization

    Human HLA-DQA1*03:02&DQB1*03:03 Monomer Protein, produced by co-expression of HLA-DQA1*03:02 and HLA-DQB1*03:03, has a calculated MW of 27.7 kDa (HLA-DQA1*03:02) and 30.2 kDa (HLA-DQB1*03:03). Subunit HLA-DQA1*03:02 is fused with a polyhistidine tag at the C-terminus and subunit HLA-DQB1*03:03 is fused with a twin strep tag at the C-terminus. The reducing (R) protein migrates as 33-42 kDa due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >90% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
HLA-DQA1*03:02 | DQB1*03:03 SDS-PAGE

Human HLA-DQA1*03:02&DQB1*03:03 Monomer Protein on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90%.

  • Background
    Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading.
  • Clinical and Translational Updates

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