| Cat # | Size | Price | Quantity | |
|---|---|---|---|---|
| 509001 | 1 mg | $160 | ||
| 509002 | 5 mg | $400 | ||
| 509003 | 25 mg | $1100 |
| Clone | PC61.5.3 |
|---|---|
| Application | ELISA, WB, Flow cytometry, IHC, ICC, animal model study |
| Host Species | CHO cells |
| Reactivity | Mouse |
| Format | Liquid |
| Target Name | mouse CD25, IL-2RA |
| Product Description | In vivo Grade Recombinant Anti-mouse CD25 Monoclonal Antibody |
| Isotype | Rat IgG1 Lambda |
| Antibody Type | Recombinant |
| Regulatory Status | RUO |
| Purity | >95% by reducing SDS-PAGE |
| Endotoxin | < 1 EU per 1 mg of the protein by the LAL method. |
| Storage Conditions | 4ºC |
| Grade | In vivo |
| Recommended Usage | This product is suitable for in vivo animal use. Optimal amounts need to be determined empirically for each experiment. |
| See All Formats | Clone PC61.5.3 |
CD25, also known as the interleukin-2 receptor alpha chain (IL-2Rα), is a transmembrane glycoprotein that plays a central role in regulating immune responses. It functions as part of the interleukin-2 (IL-2) receptor complex, which is essential for T cell proliferation, survival, and differentiation. CD25 itself has low affinity for IL-2 when expressed alone, but when combined with IL-2 receptor beta (CD122) and the common gamma chain (CD132), it forms the high-affinity IL-2 receptor complex capable of effective signal transduction.
Structurally, CD25 is a single-pass type I membrane protein composed of an extracellular domain of approximately 219 amino acids responsible for IL-2 binding, a hydrophobic transmembrane segment, and a short cytoplasmic tail that lacks intrinsic signaling domains. The extracellular region is heavily glycosylated, which stabilizes its conformation and facilitates ligand interaction. Because the alpha chain alone is not signaling-competent, it acts primarily to increase the receptor complex’s affinity for IL-2 and to expand the range of cells responsive to low cytokine concentrations.
CD25’s main ligand, IL-2, is a cytokine crucial for T lymphocyte expansion and immune tolerance. Engagement of IL-2 with the high-affinity receptor triggers the JAK-STAT signaling pathway, leading to cell proliferation, differentiation, and regulatory T cell (Treg) function. CD25 is constitutively expressed on Tregs and upregulated on activated CD4+ and CD8+ T cells, making it a marker of immune activation as well as immune regulation.
Aberrant CD25 expression or IL-2 signaling contributes to immune dysregulation and disease. In autoimmune disorders such as multiple sclerosis and type 1 diabetes, alterations in the IL-2/CD25 axis impair Treg function and tolerance mechanisms. Elevated CD25 expression is also found in certain malignancies, particularly adult T-cell leukemia/lymphoma and Hodgkin lymphoma, where it may serve as a biomarker of malignant proliferation. Moreover, soluble CD25, released from cell surfaces, can act as a decoy receptor, modulating IL-2 availability and contributing to immune suppression in cancer and chronic inflammation.
Therapeutically, CD25 is a prominent target for immune modulation. Monoclonal antibodies such as basiliximab and daclizumab have been developed to block IL-2 binding, preventing T cell activation and mitigating graft rejection in organ transplantation. Conversely, IL-2 or CD25-targeted therapies that enhance regulatory T cell function are being explored to treat autoimmune diseases and promote immune tolerance. Thus, CD25 remains a critical immunological node, balancing activation and regulation within the immune system.
In Vivo Star Anti-Mouse CD25 (IL-2Rα) Antibody TDS
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