SPR with Biotinylated Cynomolgus IFN alpha/beta R1 Protein 2042

Biotinylated Cynomolgus IFN alpha/beta R1 Protein 2042

$525.00 – $1,750.00

Summary

Expression: HEK293
Binding assay: Yes (SPR)
Amino Acid Range: Ala25-Lys437

SKU: 2042parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
molecular weight	The protein has a predicted MW of 50.35 kDa. Due to glycosylation, the protein migrates to 75-105 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Biotinylated Cynomolgus IFN alpha/beta R1 Protein 2042

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
Protein names Interferon alpha/beta receptor 1 (IFN-R-1) (IFN-alpha/beta receptor 1) (Type I interferon receptor 1)
Gene names IFNAR1,IFNAR1
Protein family Type II cytokine receptor family
Mass 9541Da
Function Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade. Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway.
Subellular location Cell membrane ; Single-pass type I membrane protein. Late endosome. Lysosome. Endosome. Membrane ; Single-pass type I membrane protein. Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes.
Structure Heterodimer with IFNAR2.
Target Relevance information above includes information from UniProt accession: A0A7N9D7J0
The UniProt Consortium

Data

SPR with Biotinylated Cynomolgus IFN alpha/beta R1 Protein

Biotinylated-Cynomolgus IFN alpha/beta R1, His-Avi Tag captured on CM5 Chip via Anti-His Antibody can bind Human IFN alpha 1, hFc Tag with an affinity constant of 1.26 nM as determined in SPR assay (Biacore T200).

HPLC of Biotinylated Cynomolgus IFN alpha/beta R1 Protein

The purity of Biotinylated Cynomolgus IFN alpha/beta R1 is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Biotinylated Cynomolgus IFN alpha/beta R1 Protein

Biotinylated Cynomolgus IFN alpha/beta R1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.