Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to
worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting
immunostaining in relation to complex human pathologies.
TCR Screening Services
Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding.
Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".
Purified / Lyophilized / Endotoxin Level: Less than 1.0 EU/µg protein (determined by LAL method).
IL2RA / CD25
42 kDa (SDS-PAGE)
Interleukin-2 receptor (IL-2R) is a heterotrimeric protein expressed on the surface of certain immune cells, such as lymphocytes, that binds and responds to the cytokine IL-2. The IL-2R is made up of 3 subunits - alpha (a), beta (ß) and gamma (?). The a and ß chains are involved in binding IL-2, while signal transduction following cytokine interaction is carried out by the ?-chain, along with the ß subunit. The ß and ? chains of the IL-2R are members of the type I cytokine receptor family. IL-2R has a high binding affinity to IL-2 and is expressed by antigen-activated T lymphocytes (T cells). IL-2 Ra is also known as CD25, p55, and Tac (activated T cell) antigen. Recombinant Human Interleukin-2 Receptor a (IL-2 R a), His produced in HEK 293 cells is a polypeptide chain containing 205 amino acids. A fully biologically active molecule, rhIL-2 R a has a molecular mass of 42 kDa analyzed by reducing SDS-PAGE and is obtained by chromatographic techniques.
The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis.