| Reactivity | HuSpecies Glossary |
| Applications | Binding Activity |
| Format | Carrier-Free |
| Details of Functionality | Measured by its binding ability in a functional ELISA. When Recombinant Human IL‑7 R alpha /CD127 Fc Chimera
(0.25 µg/mL, 100 µL/well) is immobilized on a goat anti‑human IgG Fc antibody (Catalog # G-102-C) coated plate, the concentration of recombinant human IL-7 that produces 50% of the optimal binding response is found to be 7.5-60 ng/mL. |
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| Source | Mouse myeloma cell line, NS0-derived human IL-7R alpha/CD127 protein
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| Accession # | |||||||
| N-terminal Sequence | Glu21 |
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| Structure / Form | Disulfide-linked homodimer |
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| Protein/Peptide Type | Recombinant Proteins |
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| Gene | IL7R |
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| Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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| Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
| Dilutions |
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| Theoretical MW | 54.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
|
| SDS-PAGE | 80-90 kDa, reducing conditions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Interleukin 7 Receptor alpha (IL-7 R alpha ), also known as CD127, is a 75 kDa hematopoietin receptor superfamily member that plays an important role in lymphocyte differentiation, proliferation, and survival (1, 2). Mature human IL-7 R alpha consists of a 219 amino acid (aa) extracellular domain (ECD) with one fibronectin type-III domain and a WSXWS motif, a 25 aa transmembrane segment, and a 195 aa cytoplasmic domain (3). Alternate splicing of human IL-7 R alpha generates a secreted soluble form of the receptor (3). Within the ECD, human IL‑7 R alpha shares 67% aa sequence identity with mouse and rat IL-7 R alpha . IL-7 R alpha associates with the common gamma chain ( gamma c) to form the functional high affinity IL-7 receptor complex (4). The gamma c is also a subunit of the receptors for IL-2, -4, -9, -15, and -21. Human and mouse IL‑7 show cross-species activity through the IL-7 receptor (3, 5). IL-7 R alpha is expressed on double negative (CD4-/CD8-) and CD4+ or CD8+ single positive T cells as well as on CD8+ memory T cells and their precursors (6, 7). It is expressed early in B cell development, prior to the appearance of surface IgM (6). In mouse, IL-7 activation of IL-7 R alpha is critical for both T cell and B cell lineage development (8). In human, by contrast, it is required for T cell but not for B cell development (9). IL-7 induces the downregulation and shedding of cell surface IL‑7 R alpha (10). IL-7 R alpha additionally associates with TSLP R to form the functional receptor for thymic stromal lymphopoietin (11, 12). TSLP indirectly regulates T cell development by modulating dendritic cell activation (2, 13). Knockout of TSLP R in mice provokes minor changes in B and T cell development compared to those seen with IL-7 R alpha deletion (8, 14). The complexity of IL-7 R alpha biology is suggested by the competition between IL-7 and TSLP for receptor binding and by the ability of IL-7 R alpha to form functional complexes with SCF R and HGF R (11, 12, 15, 16).
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| Gene Symbol | IL7R |
| Uniprot |
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