Recombinant Human TSLPR His-tag Avi-tag Protein, CF
Recombinant Human TSLPR His-tag Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human TSLPR (Gly25-Lys231) Accession # Q9HC73.1 | 6-His tag | Avi-tag |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
AVI10843
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 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.
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Scientific Data
2 μg/lane of Biotinylated Recombinant Human TSLPR His-tag Avi-tag Protein (Catalog # AVI10843) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 40-55 kDa.
Reconstitution Calculator
Background: TSLPR
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 ( gamma c) 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.
- Park LS et al. (2000) J. Exp. Med. 192:659.
- Blagoev, B. et al. (2002) Gene. 284:161.
- Ziegler, S.F. et al. (2013) Advances in Pharmacology. 66:129.
- He, R. et al. (2010) Ann N Y Acad Sci. 1183:13.
- Hiroyama, T. et al. (2000) Biochem. Biophys. Res. Commun. 272:224.
- Headley, M.B. et al. (2009) J Imunol. 182:1641.
- Soumelis, V. et al. (2002) Nat Immunol. 3:673.
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