Recombinant Rat TIM-3 Fc Chimera Protein, CF Summary
|Rat TIM-3 |
Accession # P0C0K5.2
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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 250 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.
2 μg/lane of Recombinant Rat TIM-3 Fc Chimera Protein (10489-TM) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 60-75 kDa and 120-150 kDa, respectively.
T cell immunoglobulin and mucin domain-3 (TIM-3) also known as HAVCR2, is a member of the TIM family of immune regulating molecules. TIMs are type I transmembrane glycoproteins with one Ig-like V-type domain, a Ser/Thr-rich mucin stalk region (1, 2). While lacking a specific immunoreceptor tyrosine-based inhibition motif (ITIM), the cytoplasmic domain of TIM-3 contains a conserved region of five tyrosine residues important for downstream signaling (3). A soluble form of TIM-3 lacking the mucin stalk and transmembrane domains is formed as either a result of alternative splicing or metalloproteinase-dependent cleavage. Within the ECD, mature rat TIM-3 shares 60% and 69% amino acid sequence identity with human and mouse TIM-3, respectively. 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 (3,11). 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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