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CD8/CD8 alpha/Leu-2  Protein, Antibody, ELISA Kit, cDNA Clone

Description: Active  
Expression host: Human Cells  
  • Slide 1
10980-H08H-20
10980-H08H-10
20 µg 
10 µg 
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Description: Active  
Expression host: Human Cells  
  • Slide 1
50389-M08H-50
50389-M08H-20
50 µg 
20 µg 
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Expression host: Human Cells  
  • Slide 1
80285-R02H-20
80285-R02H-100
20 µg 
100 µg 
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Description: Active  
Expression host: Human Cells  
  • Slide 1
60001-F08H-50
60001-F08H-100
50 µg 
100 µg 
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CD8/CD8 alpha/Leu-2 Related Area

CD8/CD8 alpha/Leu-2 Related Pathways

    CD8/CD8 alpha/Leu-2 Related Protein, Antibody, cDNA Gene, and ELISA Kits

    CD8/CD8 alpha/Leu-2 Summary & Protein Information

    CD8/CD8 alpha/Leu-2 Background

    Gene Summary: The CD8 antigen is a cell surface glycoprotein found on most cytotoxic T lymphocytes that mediates efficient cell-cell interactions within the immune system. The CD8 antigen acts as a coreceptor with the T-cell receptor on the T lymphocyte to recognize antigens displayed by an antigen presenting cell in the context of class I MHC molecules. The coreceptor functions as either a homodimer composed of two alpha chains or as a heterodimer composed of one alpha and one beta chain. Both alpha and beta chains share significant homology to immunoglobulin variable light chains. This gene encodes the CD8a chain. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Nov 2011]
    General information above from NCBI
    Subunit structure: In general heterodimer of an alpha and a beta chain linked by two disulfide bonds. Can also form homodimers. Shown to be expressed as heterodimer on thymocytes and as homodimer on peripheral blood T-lymphocytes. Interacts with the MHC class I HLA-A/B2M dimer. Interacts with LCK in a zinc-dependent manner.
    Domain: The C-terminal domain is necessary for retention within intracellular membranes (By similarity).
    Subcellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein.
    Isoform 2: Secreted.
    Post-translational: All of the five most C-terminal cysteines form inter-chain disulfide bonds in dimers and higher multimers, while the four N- terminal cysteines do not (By similarity).
    Involvement in disease: Familial CD8 deficiency (CD8 deficiency) [MIM:608957]: Novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections. Note=The disease is caused by mutations affecting the gene represented in this entry.
    Sequence similarity: Contains 1 Ig-like V-type (immunoglobulin-like) domain.
    General information above from UniProt

    Human T-cell surface glycoprotein CD8 alpha chain, also known as CD8a, is a single-pass type I  membrane protein. The CD8 glycoprotein is expressed by thymocytes, mature T cells and natural killer (NK) cells and has been implicated in the recognition of monomorphic determinants on major histocompatibility complex (MHC) Class I antigens, and in signal transduction during the course of T-cell activation. Both human and rodent CD8 antigens are comprised of two distinct polypeptide chains, alpha and beta. The Ig domains of CD8 alpha are involved in controlling the ability of CD8 to be expressed. Mutation of B- and F-strand cysteine residues in CD8 alpha reduced the ability of the protein to fold properly and, therefore, to be expressed. Defects in CD8A are a cause of familial CD8 deficiency. Familial CD8 deficiency is a novel autosomal recessive immunologic defect characterized by absence of CD8+ cells, leading to recurrent bacterial infections.

    CD8/CD8 alpha/Leu-2 Alternative Name

    CD8 alpha,Leu-2,p32 186910 , []
    p32,CD8,MAL,Leu2, [homo-sapiens]
    CD8A,Leu2,CD8,MAL,p32, [human]
    CD8a,BB154331,Ly-2,Ly-35,Ly-B,Lyt-2, [mouse]
    Ly-2,Ly-B,Ly-35,Lyt-2,BB154331, [mus-musculus]

    CD8/CD8 alpha/Leu-2 Related Studies

    References Devine, L. et al., 2000, J Immunol. 164 (2): 833-8. Arcaro, A. et al., 2000, J Immunol. 165 (4): 2068-76. Saha, K. et al., 2001, Nat Med. 7 (1): 65-72. Romero, P. et al., 2005, Eur J Immunol. 35 (11): 3092-4.
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