Recombinant Human TIM-3 His-tag Protein, CF Summary
Ser22-Arg200, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 200 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human Galectin-9 (Catalog # 2045-GA) is immobilized at 1 µg/mL (100 µL/well), it binds to Recombinant Human TIM-3 (Catalog # 10241-TI) with an ED50 of 0.065-0.65 µg/mL.
2 μg/lane of Recombinant Human TIM-3 Hist-tag (Catalog # 10241-TI) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 40-50 kDa.
TIM-3 (T cell immunoglobulin and mucin domain-3), also known as HAVCR2, is a 60 kDa member of the TIM family of immune regulating molecules. TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain and a Ser/Thr-rich mucin stalk region (1, 2). Mature human TIM-3 consists of a 181 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 78 aa cytoplasmic tail (3). An alternatively spliced isoform is truncated within the mucin-like stalk. Within the ECD, human TIM-3 shares 58% aa sequence identity with mouse and rat TIM-3. TIM-3 is up‑regulated on several populations of activated myeloid cells (macrophage, monocyte, dendritic cell, microglia, mast cell) and T cells (Th1, CD8+, NK, Treg) (3-10). Its binding to Galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity (11). TIM-3 ligation attenuates CD8+ and Th1 cell responses (11-13) and promotes the activity of Treg and myeloid derived suppressor cells (8, 11, 13, 14). In addition, dendritic cell-expressed TIM-3 dampens inflammation by enabling the phagocytosis of apoptotic cells and the cross-presentation of apoptotic cell antigens (4). It also binds the alarmin HMGB1, thereby preventing the activation of TLRs in response to released tumor cell DNA (7). TIM-3 interactions with Galectin-9 can alternatively trigger immune stimulatory effects, such as the coactivation of NK cell cytotoxicity (10).
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