Rat Anti-Cd8b1 Recombinant Antibody (clone YTS156.7.7)
CAT#: HPAB-S0182-YC
This is a rat antibody binds to Cd8b1. The mAb inhibits and prevents T cell activation. Epitopes on CD8β have been identified, implying that residues in the CDR1 and CDR2 equivalent loops of CD8β are blocked upon binding to class I pMHC.
Gene Expression
Published Data
Subcellular Location
Figure 1 IF staining of human cell line CACO-2
Immunofluorescent staining of human cell line CACO-2 shows localization to plasma membrane.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/29164/1526_E8_1_selected.jpg
Normal Tissue
Figure 2 High expression in lymph node.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/4353/165972_A_9_8_val_selected.jpg
Normal Tissue
Figure 3 Low expression in liver.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/4353/165972_A_9_4_val_selected.jpg
Normal Tissue
Figure 4 Lymph node
Germinal center cells Staining: Medium Intensity: Strong Quantity: <25% Location: Cytoplasmic/ membranous Non-germinal center cells Staining: Medium Intensity: Strong Quantity: <25% Location: Cytoplasmic/ membranous
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/images/4353/165972_A_9_8.jpg
RNA Expression
Figure 5 RNA cell line category: Cell line enriched (RPMI-8226)
Cell lines ordered by descending RNA expression order.
* Image credit: Image credit: Human Protein Atlas https://v21.proteinatlas.org/ENSG00000172116-CD8B
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FC
Figure 1 CD8-β is a target of ART2.2-mediated ADP-ribosylation.
In the liver, the CD8-α+ T cells displayed strong staining with the anti-CD8-β mAb H35-17.2, but reduced staining with the anti-CD8-β mAb YTS156.7.7 and 53-5.8.
Lischke, T., Schumacher, V., Wesolowski, J., Hurwitz, R., Haag, F., Koch‐Nolte, F., & Mittrücker, H. W. (2013). CD 8‐β ADP‐ribosylation affects CD 8+ T‐cell function. European Journal of Immunology, 43(7), 1828-1838.
FC
Figure 2 The anti-CD8-β mAb clones YTS156.7.7 and 53-5.8 do not recognize CD8-β in the presence of extracellular NAD+.
ART2.2 transfers ADP-ribose from extracellular NAD+ onto arginine residues of adjacent surface proteins. Incubation of splenic CD8+ T cells with NAD+ resulted in a concentrationdependent loss of binding of the anti-CD8-β mAb YTS156.7.7 and 53-5.8, but not of mAb H35-17.2 or of the anti-CD8-α mAb 53-6.7.
Lischke, T., Schumacher, V., Wesolowski, J., Hurwitz, R., Haag, F., Koch‐Nolte, F., & Mittrücker, H. W. (2013). CD 8‐β ADP‐ribosylation affects CD 8+ T‐cell function. European Journal of Immunology, 43(7), 1828-1838.
FC
Figure 3 CD8-β ADP-ribosylation is stable in vivo for up to 24 h.
Spleen cells were incubated in vitro with 100 μM NAD+, and the ADP-ribosylation was determined with anti-CD8-β mAb at different time points after the start of NAD+ treatment. After 30 min, we observed substantial loss of staining with the sensitive anti-CD8-β mAb YTS156.7.7 and mAb 53-5.8.
Lischke, T., Schumacher, V., Wesolowski, J., Hurwitz, R., Haag, F., Koch‐Nolte, F., & Mittrücker, H. W. (2013). CD 8‐β ADP‐ribosylation affects CD 8+ T‐cell function. European Journal of Immunology, 43(7), 1828-1838.
FC
Figure 4 ADP-ribosylation of CD8-β is enhanced in the absence of CD38.
Spleen cells from CD38 KO mice showed profoundly reduced staining levels for the sensitive anti-CD8-β mAb YTS156.7.7 and 53-5.8, and treatment of mice with NAD+ prior to spleen cell isolation resulted in a further decline in the staining intensity.
Lischke, T., Schumacher, V., Wesolowski, J., Hurwitz, R., Haag, F., Koch‐Nolte, F., & Mittrücker, H. W. (2013). CD 8‐β ADP‐ribosylation affects CD 8+ T‐cell function. European Journal of Immunology, 43(7), 1828-1838.
FC
Figure 5 CD8-β ADP-ribosylation occurs during cell isolation.
For all analyzed tissues, we consistently observed lower staining levels for the sensitive anti-CD8-β mAb for cells from WT mice when compared to cells from ART2 KO mice.
Lischke, T., Schumacher, V., Wesolowski, J., Hurwitz, R., Haag, F., Koch‐Nolte, F., & Mittrücker, H. W. (2013). CD 8‐β ADP‐ribosylation affects CD 8+ T‐cell function. European Journal of Immunology, 43(7), 1828-1838.
Figure 6 YTS156.7.7, but not YTS105.18, blocks MHC class I and CD8 interaction and subsequent T cell activation.
Incubation of OT-1 T cells with YTS156.7 mAb prior to tetramers of H-2Kb/OVA completely blocked calcium flux, indicating inhibition of pMHCI/CD8 interaction.
Shore, D. A., Issafras, H., Landais, E., Teyton, L., & Wilson, I. A. (2008). The crystal structure of CD8 in complex with YTS156. 7.7 Fab and interaction with other CD8 antibodies define the binding mode of CD8 αβ to MHC class I. Journal of molecular biology,384(5), 1190-1202.
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Specifications
- Host Species
- Rat
- Type
- Rat IgG
- Specificity
- Mouse CD8B
- Species Reactivity
- Mouse
- Clone
- YTS156.7.7
- Applications
- Neut
Product Property
- Purity
- >95% as determined by SDS-PAGE and HPLC analysis
- Buffer
- PBS
- Storage
- Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Target
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Product Notes
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
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MSDS
COA
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| CAT | Product Name | Application | Type |
|---|---|---|---|
| FAMAB-0012-CN-F(E) | Mouse Anti-CD8B Recombinant Antibody (clone EP42); Fab Fragment | FC | Mouse Fab |
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| CAT | Product Name | Application | Type |
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