EPX Monoclonal / Janelia Fluor 646 / EPO104
Product Details
| Description | Peripheral blood granulocytes are classified into neutrophils, basophils and eosinophils according to the staining characteristics of their cytoplasmic granules. Granule proteins are released by physiologic and pharmacologic stimuli and play important roles in both normal and pathological host immune responses. Eosinophil major basic protein and eosinophil peroxidase (EPX) are granule proteins specific to the eosinophil. AHE-1 recognizes human EPX, a granule protein specific to eosinophils. It does not cross-react with eosinophil major basic protein, elastase, cathepsin G, esterase N, thrombin, plasmin, kallikrein, lactoferrin, or transferrin. This MAb stains eosinophils only and does not stain other peripheral blood cells, including platelets, neutrophils, monocytes, lymphocytes or red blood cells. Human EPX gene product can form a tetramer of two light chains and two heavy chains. Other peroxidase family members include myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). | |
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| Conjugate | Janelia Fluor 646 | |
| Clone | EPO104 | |
| Target Species | Human | |
| Applications | FC, ICC, IF, IHC-Fr, IHC | |
| Supplier | Novus Biologicals | |
| Catalog # | Sign in to view product details, citations, and spectra | |
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About EPX
This gene is a member of the peroxidase gene family and is expressed in eosinophils. The encoded preproprotein is proteolytically processed into covalently attached heavy and light chains to form the mature enzyme, which functions as an oxidant. The enzyme is released at sites of parasitic infection or allergen stimulation to mediate lysis of protozoa or parasitic worms. The gene is found in a gene cluster with other peroxidase genes on chromosome 17. Mutations in this gene result in eosinophil peroxidase deficiency. [provided by RefSeq, Feb 2016]
This gene is a member of the peroxidase gene family and is expressed in eosinophils. The encoded preproprotein is proteolytically processed into covalently attached heavy and light chains to form the mature enzyme, which functions as an oxidant. The enzyme is released at sites of parasitic infection or allergen stimulation to mediate lysis of protozoa or parasitic worms. The gene is found in a gene cluster with other peroxidase genes on chromosome 17. Mutations in this gene result in eosinophil peroxidase deficiency. [provided by RefSeq, Feb 2016]
About Janelia Fluor 646
Janelia Fluor® 646 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 646 has an excitation peak at 646 nm and an emission peak at 664 nm.
Janelia Fluor® 646 was developed at the Janelia Campus of the Howard Hughes Medical Institute but is commercialized by other vendors. The Janelia Fluor®s family is unique in that the fluorophores are cell-permeable and are available in photoactivatable forms. These fluorophores were developed for super-resolution microscopy (STED, PALM and STORM) and live-cell microscopy in the HaloTag and SNAP-tag versions. Janelia Fluor® 646 has an excitation peak at 646 nm and an emission peak at 664 nm.
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