Anti-Human CD25 (IL-2R) (Daclizumab) [Clone Hu102]
Anti-Human CD25 (IL-2R) (Daclizumab) [Clone Hu102]
Product No.: C2510
Product No.C2510 Clone Hu102 Target CD25 Product Type Biosimilar Recombinant Human Monoclonal Antibody Alternate Names IL2RA, IL2R, p55, TAC Isotype Human IgG1κ Applications ELISA , FC , IHC , WB |
Antibody DetailsProduct DetailsReactive Species Human Host Species Human Expression Host HEK-293 Cells FC Effector Activity Active Immunogen Humanized antibody derived from mouse clone that binds to Human CD25. Product Concentration ≥ 5.0 mg/ml Endotoxin Level < 1.0 EU/mg as determined by the LAL method Purity ≥95% by SDS Page ⋅ ≥95% monomer by analytical SEC Formulation This biosimilar antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration. State of Matter Liquid Product Preparation Recombinant biosimilar antibodies are manufactured in an animal free facility using only in vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates. Pathogen Testing To protect mouse colonies from infection by pathogens and to assure that experimental preclinical data is not affected by such pathogens, all of Leinco’s recombinant biosimilar antibodies are tested and guaranteed to be negative for all pathogens in the IDEXX IMPACT I Mouse Profile. Storage and Handling Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one month. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≤ -70°C. Avoid Repeated Freeze Thaw Cycles. Regulatory Status Research Use Only Country of Origin USA Shipping 2 – 8° C Wet Ice Additional Applications Reported In Literature ? ELISA, FC, WB, IHC Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. DescriptionDescriptionSpecificity This non-therapeutic biosimilar antibody uses the same variable region sequence as the therapeutic antibody Daclizumab. This product is for research use only. Daclizumab activity is directed against the Tac epitope of CD25. Background Interleukin-2 receptor (IL-2R), which regulates normal immune function 1 and is involved in signal transduction, cell growth and survival 2 , is composed of CD25, CD122, and CD132 3 . CD25 is the alpha-chain of IL-2R 2 and its expression is upregulated in resting T cells after activation, which in turn increases the binding capacity of IL-2 and positively affects signaling for T cell proliferation and survival 4. Daclizumab prevents the formation of the heterotrimeric IL-2R and selectively blocks IL-2R-mediated signaling 3 . By masking the IL-2 binding site on IL-2R, daclizumab inhibits T cell activation and proliferation as well as prevents IL-2 from stimulating Tregs to induce apoptosis in effector T cells 4. Additionally, daclizumab can remove CD25 from the surfaces of T cells via monocyte-dependent trogocytosis (defined as the active transfer of plasma membrane fragments between two live cells triggered by interaction between a cognate antigen on one cell and an antigen receptor signaling pathway on another cell) 3 . Daclizumab also inhibits activation and proliferation of T cells by blocking dendritic cells from presenting IL-2 to resting T cells 4 . Daclizumab reduces T cell CD25 levels via a mechanism that requires Fc domain interaction with FcR on monocytes, but not on natural killer cells 3 . Blocking IL-2 from binding to T cells leads to increased binding to CD56 bright NK cells via the IL-2R beta subunit 4 . This then leads to an expansion of CD56 bright NK cells, which target and kill activated T cells and is associated with reduced inflammation in the brain and decreased atrophy of brain tissue. Daclizumab is humanized anti-Tac 5, 6 and is composed of two humanized gamma-1 heavy chains and two humanized kappa light chains 4 that are sequence optimized for high affinity5, 6 . Daclizumab has been used in the treatment or prevention of a variety of autoimmune disorders and renal allograft rejection, respectively 6. Antigen Distribution CD25 is constitutively expressed at high levels on CD4+CD25+FoxP3+
regulatory T cells and at low levels on resting T cells. CD25 is expressed by approximately 30% of human peripheral blood B cells, particularly those belonging to the memory B cell population. Additionally, CD25 is expressed on the cell surface of many lymphomas and is increased within serum and the central nervous system of patients with multiple sclerosis. Ligand/Receptor IL-2 NCBI Gene Bank ID UniProt.org Research Area Biosimilars . Cancer . Immuno-Oncology . Immunology Leinco Antibody AdvisorPowered by AI: AI is experimental and still learning how to provide the best assistance. It may occasionally generate incorrect or incomplete responses. Please do not rely solely on its recommendations when making purchasing decisions or designing experiments. Research-grade Daclizumab biosimilars are used as calibration standards or reference controls in pharmacokinetic (PK) bridging ELISA by preparing a standard curve, against which the concentrations of Daclizumab in patient serum samples are measured. The biosimilar is typically validated to ensure its bioanalytical equivalence to the reference product, allowing both biosimilar and reference samples to be measured accurately in the same assay. Context and supporting details:
Additional Notes:
In summary: Research-grade Daclizumab biosimilars, after validation for equivalence, are routinely used to generate standard curves and serve as quality controls in PK bridging ELISA assays, providing the quantitative basis to measure both reference and biosimilar drug in serum. Research-grade anti-CD25 antibodies are primarily studied in syngeneic mouse models for tumor growth inhibition and TIL characterization, with limited use of humanized models. These models serve as critical platforms for evaluating CD25-targeted immunotherapy approaches that aim to deplete regulatory T cells (Tregs) within the tumor microenvironment. Syngeneic Mouse ModelsSyngeneic models represent the gold standard for anti-CD25 antibody research due to their preserved immune system integrity. These models involve implanting murine tumors into immunocompetent mice, which maintains the native immune system while enabling TIL expansion and response to therapy. The key advantage is that syngeneic models preserve the complex interactions between the immune system and tumor that are essential for studying CD25-targeted approaches. Commonly Used Syngeneic Tumor Models include MC38, Hepa1-6, CT-26, and EMT-6, which have been systematically characterized for their responsiveness to immunotherapy interventions. In the mouse A20 lymphoma model specifically, anti-mouse CD25 monoclonal antibodies (PC61) have been tested, though they showed limited tumor growth inhibition when administered after tumor establishment. Administration Approaches in syngeneic models vary significantly in their effectiveness. Systemic administration of anti-CD25 antibodies before tumor challenge has demonstrated tumor growth inhibition and improved survival. However, direct intratumoral injection has emerged as a more effective strategy. When anti-CD25 immunotoxins are injected directly into tumors, they achieve concentrations around 100 μg/mL in the tumor microenvironment, causing significant tumor regressions and development of antitumor immunity across multiple tumor models. Novel Delivery SystemsRecent innovations have expanded beyond traditional antibody administration to include implantable anti-CD25 systems. Researchers have developed anti-CD25 antibody-immobilized polyethylene meshes that can be surgically implanted near tumors. In tumor-bearing mice, subcutaneous implantation of these CD25-PE meshes for one week successfully suppressed tumor growth by capturing Tregs locally. This approach demonstrates enhanced Treg capture around the implanted fibers and shows promise for localized immunotherapy. Humanized Mouse ModelsWhile syngeneic models dominate the field, humanized mouse models are being developed to better recapitulate human immune-tumor interactions. These models introduce human immune cells, including TILs, into immunodeficient mice to mimic human immune responses. However, the literature shows limited specific applications of research-grade anti-CD25 antibodies in fully humanized systems, likely due to the technical challenges of maintaining functional human immune components. Two novel human anti-CD25 antibodies, BA9 and BT942, have been identified and characterized for their antitumor activity. These antibodies demonstrated significant tumor growth inhibition in both early and late-stage animal cancer models, with BT942 showing particularly effective CD8+ T cell expansion despite weaker binding affinity compared to BA9. Clinical Translation ConsiderationsThe research consistently emphasizes that syngeneic models provide the most physiologically relevant platform for evaluating anti-CD25-based therapies before clinical translation. These models effectively preserve the native immune system architecture necessary for studying TIL dynamics and immune responses to CD25 targeting, making them indispensable for characterizing both the therapeutic efficacy and immunological mechanisms of anti-CD25 interventions in cancer immunotherapy development. Researchers investigate combination immunotherapy—including the use of Daclizumab biosimilars (anti-CD25) with other checkpoint inhibitors such as anti-CTLA-4 or anti-LAG-3 biosimilars—primarily in preclinical and clinical immune-oncology models to evaluate synergistic antitumor effects. However, robust published evidence specifically on Daclizumab biosimilars in these combinations is limited, and most peer-reviewed synergy studies focus on more established checkpoint inhibitors. Essential context and supporting details:
Summary Table: Synergy Study Approaches in Immune-Oncology Models
For further insights, ongoing clinical trial registries and conference proceedings may provide unpublished or preliminary data regarding such combination strategies. In a bridging ADA ELISA for immunogenicity testing, a Daclizumab biosimilar can be used as both the capture and detection reagent to specifically detect anti-drug antibodies (ADAs) that a patient generates against Daclizumab therapy. How a Daclizumab biosimilar is used in a bridging ADA ELISA:
Thus, any detected signal (e.g., colorimetric change) indicates the presence of antibodies in the patient sample that bind Daclizumab, monitoring the immune response against the drug. Key principles and considerations:
Regulatory context:
Summary Table:
By using the Daclizumab biosimilar in both roles, this bridging ELISA sensitively monitors the patient's immune response to the therapeutic, ensuring detection of potentially clinically relevant ADAs. References & Citations1 Zammarchi F, Havenith K, Bertelli F, et al. J Immunother Cancer. 8(2):e000860. 2020. 2 Epperla N, Hamadani M. Curr Hematol Malig Rep. 16(1):19-24. 2021. 3 Zhang Y, McClellan M, Efros L, et al. Mult Scler. 20(2):156-164. 2014. 4 Kim AP, Baker DE. Hosp Pharm. 51(11):928-939. 2016. 5 Queen C, Schneider WP, Selick HE, et al. Proc Natl Acad Sci U S A. 86(24):10029-10033. 1989. 6 Waldmann TA. J Clin Immunol. 27(1):1-18. 2007. 7 Vincenti F, Kirkman R, Light S, et al. N Engl J Med. 338(3):161-165. 1998. 8 Beniaminovitz A, Itescu S, Lietz K, et al. N Engl J Med. 342(9):613-619. 2000. 9 Krueger JG, Walters IB, Miyazawa M, et al. J Am Acad Dermatol. 43(3):448-458. 2000. 10 Phillips KE, Herring B, Wilson LA, et al. Cancer Res. 60(24):6977-6984. 2000. 11 Maciejewski JP, Sloand EM, Nunez O, et al. Blood. 102(10):3584-3586. 2003. 12 Zhang M, Zhang Z, Garmestani K, et al. Cancer Res. 64(16):5825-5829. 2004. 13 Kobashigawa J, David K, Morris J, et al. Transplant Proc. 37(2):1333-1339. 2005. 14 Sloand EM, Scheinberg P, Maciejewski J, et al. Ann Intern Med. 144(3):181-185. 2006. 15 Bielekova B, Catalfamo M, Reichert-Scrivner S, et al. Proc Natl Acad Sci U S A. 103(15):5941-5946. 2006. 16 Kappos L, Wiendl H, Selmaj K, et al. N Engl J Med. 373(15):1418-1428. 2015. Technical ProtocolsCertificate of Analysis |
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