Recombinant Human TSLPR Fc Chimera Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. Measured by its binding ability in a functional ELISA. When Recombinant Human TSLP
(Catalog #
1398-TS)
is immobilized at 0.5 μg/mL (100 μL/well), the concentration of
Biotinylated Recombinant Human TSLP Fc Chimera Avi-tag (Catalog #
AVI981) that produces 50% of the optimal binding response is 0.75-7.5 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human TSLPR protein
Human TSLPR (Gly25 & Val30-Lys231) Accession # Q9HC73.1 |
DIEGRMD |
Human IgG1
(Pro100-Lys330) |
Avi-tag |
N-terminus |
|
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Gly25 and Val30 |
Structure / Form |
Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
52 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
65-80 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human TSLPR Fc Chimera Avi-tag Protein, CF
Background
Thymic stromal lymphopoietin receptor (TSLPR), also known
cytokine receptor-like factor 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 (1, 2). Human TSLPR shares
34% amino acid sequence identity with 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).
- 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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