Anti-Mouse TCR β chain – Purified in vivo GOLD™ Functional Grade

Affinity purified TCR from mouse DO-11.10 cells

This monoclonal 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.

Functional grade preclinical antibodies are manufactured in an animal free facility using in vitro 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.

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 -80°C. Avoid Repeated Freeze Thaw Cycles.

Next Day 2-8°C

Clone H57-597 recognizes an epitope on the constant region of mouse TCRβ. Clone H57-597 does not cross-react with γδ T cells.

TCRβ is expressed on αβ thymocytes, peripheral T cells, and NKT cells.

TCRβ antibody, clone H57-597, recognizes the beta chain of the T cell receptor (TCRβ), expressed on αβ thymocytes and T lymphocytes, as well as natural killer T (NKT) cells¹. TCRβ is a transmembrane protein that consists of an amino-terminal variable region, a constant region, and a stalk segment covalently linked to the TCR alpha chain (TCRα) via a disulfide bond². TCRα/β does not contain signaling domains and is instead noncovalently associated with the CD3 complex (TCR-CD3), essential for TCR signaling^3,4. TCRα/β recognizes antigens bound to major histocompatibility complex (MHC) molecules, resulting in phosphorylation of CD3 ITAMs and subsequent T cell activation, proliferation, and survival^5,6.

Peptide bound-MHC class I and II

Antigen recognition, T cell activation

1. Krijgsman D, et al. (2018) Front Immunol. 9:367
2. Clevers H, et al. (1988) Annu Rev Immunol. 6:629-62
3. Kuhns MS, Badgandi HB. (2012) Immunol Rev. 250(1):120-43
4. Wucherpfennig KW, et al. (2010) Cold Spring Harb Perspect Biol. 2(4):a005140
5. Samelson LE. (2002) Annu Rev Immunol. 20:371-94
6. Borroto A, et al. (2014) Immunol Lett. 161(1):113-7