Recombinant Human TSLPR His-tag Avi-tag Protein, CF

Thymic stromal lymphopoietin receptor (TSLPR), also known cytokine receptor-like module 2 (CRLM-2) and IL-XR, is a member of the type 1 cytokine receptor family. TSLPR has been identified most closely related to the common gamma chain ( gammac) and, when complexed with interleukin 7 receptor alpha (IL-7R alpha), forms a high affinity complex for the IL-7-like cytokine TSLP (1-4). The extracellular domain (ECD) of human TSLPR contains two fibronectin type III-like domains and a WSXWS‑like motif, which is necessary for proper protein folding (1-4). The cytoplasmic domain contains a membrane-proximal box 1 motif that is important for association with JAKs (2, 3). The ECD of Human TSLPR shares 34% amino acid sequence identity with the ECD of mouse TSLPR. An alternatively spliced mRNA variant encoding a soluble TSLPR has also been reported in mouse (5). In the signaling pathway of TSLP-TSLPR, which is similar to that of IL-7, TSLP activates the transcription factor signal transducer and activator of transcription 3 (STAT3), inducing the expression of common genes (4). TSLPR expression is ubiquitous in the immune and hematopoietic cells but is up-regulated in Th2-skewed cells (3, 4). Elevated expression of TSLP-TSLPR in bronchial mucosa has been associated with human asthma by acting as a susceptibility factor to generate Th2 allergic responses to antigens (4, 6). TSLP also is involved in Th2-mediated allergic skin inflammation by inducing Th2 cytokine secretion by T cells during the effector phase of allergic skin inflammation (4, 7). TSLP has been shown to induce the release of T cell-attracting chemokines from monocytes and enhance the maturation of CD11c+ dendritic cells (DC) (4). TSLP activated human DCs are also involved in the homeostatic proliferation of naïve and memory T cells in the absence of foreign antigens (4). Our Avi-tag Biotinylated Recombinant Human TSLPR protein features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.