Purified NA/LE Mouse Anti-Human CD8
Clone HIT8a (RUO)
- Brand BD Pharmingen™
- Concentration 1.0 mg/ml
- Isotype Mouse IgG1, κ
- Reactivity Human (QC Testing)
Flow cytometry (Routinely Tested)
- Workshop No. V 5T-CD08.10
- Storage Buffer No azide/low endotoxin: Aqueous buffered solution containing no preservative, 0.2µm sterile filtered. Endotoxin level is ≤0.01 EU/µg (≤0.001 ng/µg) of protein as determined by the LAL assay.
- Regulatory Status RUO
Regulatory Status Legend
The HIT8a monoclonal antibody specifically binds to CD8a (CD8α). CD8α is a type I transmembrane glycoprotein and a member of the immunoglobulin superfamily. CD8α is expressed by the majority of thymocytes, by subpopulations of αβ T cells and γδ T cells and by some NK cells. Cell surface CD8α is expressed either as a disulfide-linked homodimer (CD8αα) or as a heterodimer (CD8αβ) when disulfide-bonded to a CD8 beta chain (CD8β). CD8-positive αβ T cells coexpress both CD8αα homodimers and CD8αβ heterodimers whereas some γδ T cells and NK cells express CD8αα homodimers. CD8 plays important roles in T cell activation and selection. The extracellular IgSF domain of CD8α binds to a non-polymorphic determinant on HLA class I molecules (α3 domain) and enables CD8 to function as a coreceptor with MHC class I-restricted TCR during T cell recognition of antigen. The cytoplasmic domain of CD8α associates with Lck, a Src family protein tyrosine kinase that is involved in intracellular signaling. Clones HIT8a and RPA-T8 are not cross-blocking.
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Preparation and Storage
Store undiluted at 4°C.
The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
This preparation contains no preservatives, thus it should be handled under aseptic conditions.
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- An isotype control should be used at the same concentration as the antibody of interest.
- Please refer to www.bdbiosciences.com/pharmingen/protocols for technical protocols.