Flow cytometric analysis of Human CD90 expression on Jurkat cells. Cells from the Jurkat (Human T cell leukemia T lymphocyte, Right) or K562 (Human chronic myelogenous leukemia lymphoblast, Left) was stained with either FITC Mouse IgG1 Isotype Control (Black line histogram) or SDT FITC Mouse Anti-Human CD90 antibody (Red line histogram) at 0.25 μg/test, cells without incubation with primary antibody and secondary antibody (Blue line histogram) was used as unlabelled control. Flow cytometry and data analysis were performed using BD FACSymphony™ A1 and FlowJo™ software.
FITC Mouse anti-Human CD90 Antibody (S-R538)
FITC Mouse anti-Human CD90 Antibody (S-R538)
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Product Details
Product Details
Product Specification
| Host | Mouse |
| Antigen | CD90 |
| Synonyms | Thy-1 membrane glycoprotein; CDw90; Thy-1 antigen, THY1 |
| Location | Cell membrane |
| Accession | P04216 |
| Clone Number | S-R538 |
| Antibody Type | Mouse mAb |
| Isotype | IgG1 |
| Application | FCM |
| Reactivity | Hu |
| Positive Sample | Jurkat |
| Purification | Protein G |
| Concentration | 0.2mg/ml |
| Conjugation | FITC |
| Physical Appearance | Liquid |
| Storage Buffer | PBS, 25% Glycerol, 1% BSA, 0.3% Proclin 300 |
| Stability & Storage | 12 months from date of receipt / reconstitution, 2 to 8 °C as supplied. |
Dilution
| application | dilution | species |
| FCM | 1.25 μl per million cells in 100μl volume | Hu |
Background
Thy-1 or CD90 (Cluster of Differentiation 90) is a ~25–37 kDa heavily N-glycosylated, glycophosphatidylinositol (GPI) anchored conserved cell surface protein with a single V-like immunoglobulin domain, originally discovered as a thymocyte antigen. Thy-1 can be used as a marker for a variety of stem cells and for the axonal processes of mature neurons. Structural study of Thy-1 led to the foundation of the Immunoglobulin superfamily, of which it is the smallest member, and led to some of the initial biochemical description and characterization of a vertebrate GPI anchor and also the first demonstration of tissue specific differential glycosylation.
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