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cd8α cd8β chains  (Azenta)

 
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    Azenta cd8α cd8β chains
    Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and <t>CD8β</t> on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.
    Cd8α Cd8β Chains, supplied by Azenta, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cd8α cd8β chains/product/Azenta
    Average 90 stars, based on 1 article reviews
    cd8α cd8β chains - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "High-affinity CD8 variants enhance the sensitivity of pMHCI antigen recognition via low-affinity TCRs"

    Article Title: High-affinity CD8 variants enhance the sensitivity of pMHCI antigen recognition via low-affinity TCRs

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2023.104981

    Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and CD8β on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.
    Figure Legend Snippet: Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and CD8β on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.

    Techniques Used: Expressing, Transduction, Functional Assay, Concentration Assay, Activation Assay, Variant Assay, Derivative Assay, SPR Assay



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    cd8α cd8β chains  (Azenta)
    90
    Azenta cd8α cd8β chains
    Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and <t>CD8β</t> on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.
    Cd8α Cd8β Chains, supplied by Azenta, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cd8α cd8β chains/product/Azenta
    Average 90 stars, based on 1 article reviews
    cd8α cd8β chains - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and CD8β on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.

    Journal: The Journal of Biological Chemistry

    Article Title: High-affinity CD8 variants enhance the sensitivity of pMHCI antigen recognition via low-affinity TCRs

    doi: 10.1016/j.jbc.2023.104981

    Figure Lengend Snippet: Design and characterization of CD8 variants. A , crystal structure of human CD8αα complexed with HLA-A∗0201 in cartoon form showing CD8α chain residue Ser53 ( red ) interacting with HLAα3 residue Asp227 ( green ). CD8α2 residue Ser53 mutations are shown in the four images below interacting with HLAα3 residue Asp227 ( green ). B , expression of TCRVβ12 and CD8β on Jurkat cells transduced with the RLA TCR and CD8αβ containing either wild-type (WT) CD8α or mutated forms (S53G, S53T, S53N, or S53Q) of CD8α. C , functional sensitivity of RLA TCR + CD8αβ + Jurkat cells expressed as the decimal cologarithm of the half-maximal efficacy concentration (pEC 50 ). The activation of RLA TCR + CD8αβ + Jurkat cells in response to C1R HLA-A2 cells pulsed with serial dilutions of the cognate peptide was assessed by measuring the upregulation of CD69. Significance was determined using a one-way ANOVA with Dunnett’s post hoc test to compare each variant versus wild-type CD8 (n = 4). Data are derived from four separate experiments. D – F , representative surface plasmon resonance affinity measurements of wild-type (WT) CD8αα ( D ) and the most functionally potent variants of CD8αα, namely S53G ( E ) and S53N ( F ), versus SLL/HLA-A∗0201.

    Article Snippet: For retroviral expression, the CD8α and CD8β chains, separated by a P2A cleavage site (Genewiz), were cloned into an MP71 vector containing an IRES sequence and a downstream expression marker (truncated NGFR).

    Techniques: Expressing, Transduction, Functional Assay, Concentration Assay, Activation Assay, Variant Assay, Derivative Assay, SPR Assay