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SLC26A3 Protein (AA 28-254) (His tag)

SLC26A3 Origin: Human Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
Catalog No. ABIN5713114
  • Target See all SLC26A3 Proteins
    SLC26A3 (Solute Carrier Family 26, Member 3 (SLC26A3))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 28-254
    Origin
    • 4
    • 1
    Human
    Source
    • 2
    • 1
    • 1
    • 1
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This SLC26A3 protein is labelled with His tag.
    Application
    SDS-PAGE (SDS)
    Sequence
    EEHVIIQAEF YLNPDQSGEF MFDFDGDEIF HVDMAKKETV WRLEEFGRFA SFEAQGALAN IAVDKANLEI MTKRSNYTPI TNVPPEVTVL TNSPVELREP NVLICFIDKF TPPVVNVTWL RNGKPVTTGV SETVFLPRED HLFRKFHYLP FLPSTEDVYD CRVEHWGLDE PLLKHWEFDA PSPLPETTEN VVCALGLTVG LVGIIIGTIF IIKGLRKSNA AERRGPL
    Purification
    SDS-PAGE
    Purity
    > 90 %
    Top Product
    Discover our top product SLC26A3 Protein
  • Application Notes
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    0.1-2 mg/mL
    Buffer
    20 mM Tris-HCl based buffer, pH 8.0
    Storage
    -80 °C,4 °C,-20 °C
    Storage Comment
    Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Target
    SLC26A3 (Solute Carrier Family 26, Member 3 (SLC26A3))
    Alternative Name
    DRA (SLC26A3 Products)
    Synonyms
    CLD Protein, DRA Protein, 9030623B18Rik Protein, 9130013M11Rik Protein, AV376035 Protein, Dra Protein, si:dkey-31f5.2 Protein, SLC26A3 Protein, solute carrier family 26 member 3 Protein, solute carrier family 26, member 3 Protein, solute carrier family 26 (anion exchanger), member 3 Protein, SLC26A3 Protein, Slc26a3 Protein, slc26a3.1 Protein
    Background
    Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents th 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 mbrane 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 syst 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 roval 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 mbrane 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.
    Molecular Weight
    29.8 kDa
    UniProt
    P01903
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