CD15 Mouse anti-Human, Brilliant Violet 650, Clone: HI98 (also known as HIM1), BD
Mouse Monoclonal Antibody
Manufacturer: BD Biosciences 564232
The HI98 monoclonal antibody specifically reacts with 3-fucosyl-N-acetyllactosamine (3-FAL), a 220 kDa carbohydrate structure, also called X-hapten, SSEA-1, CD15 or Lewis X. This structure is found on a variety of cell surface glycolipids and glycoproteins. 3-FAL is expressed on >95% of granulocytes, including neutrophils and eosinophils, and to a varying degree on monocytes, but not on lymphocytes or basophils. CD15 plays a role in mediating phagocytosis, bactericidal activity and chemotaxis. This antibody is also suitable for staining formalin-fixed, paraffin-embedded tissue sections without pretreatment. Since the Abs are recognizing a carbohydrate epitope (3-fucosyl-N-acetyllactosamine) they also should work across species and not only for human.
The antibody was conjugated to BD Horizon BV650 which is part of the BD Horizon Brilliant Violet family of dyes. This dye is a tandem fluorochrome of BD Horizon BV421 with an Ex Max of 405-nm and an acceptor dye with an Em Max at 650-nm. BD Horizon BV650 can be excited by the violet laser and detected in a filter used to detect APC-like dyes (eg, 660/20-nm filter). Due to the excitation and emission characteristics of the acceptor dye, there will be spillover into the APC and Alexa Fluor 700 detectors. However, the spillover can be corrected through compensation as with any other dye combination.
|HI98 (also known as HIM1)|
|Lewis X; Le-X; X-Hapten; SSEA-1; 3-FAL|
|Human Mononuclear Cells|
|Store undiluted at 4°C and protected from prolonged exposure to light. Do not freeze.|
|Brilliant Violet 650|
|Aqueous buffered solution containing BSA and ≤0.09% sodium azide.|
We continue to work to improve your shopping experience and your feedback regarding this content is very important to us. Please use the form below to provide feedback related to the content on this product.
Your feedback has been submitted. Fisher Scientific is always working to improve our content for you. We appreciate your feedback.Ok