IL-13R alpha 1 Protein, Mouse (Biotinylated, HEK293, Avi-His)

The IL-13R α 1 protein binds to IL13 with low affinity and, when combined with IL4RA, forms a functional IL13 receptor. It also functions together with IL4RA as an alternative accessory protein for IL4 signaling. IL-13R alpha 1 Protein, Mouse (Biotinylated, HEK293, Avi-His) is the recombinant mouse-derived IL-13R alpha 1 protein, expressed by HEK293 , with C-Avi, C-6*His labeled tag.

The IL-13R alpha 1 protein exhibits a low-affinity binding to interleukin-13 (IL13) and, when partnered with IL4RA, forms a functional receptor for IL13. Furthermore, IL-13R alpha 1 serves as an alternate accessory protein alongside IL4RA for interleukin-4 (IL4) signaling. Although it cannot replace the function of IL2RG in enabling enhanced interleukin-2 (IL2) binding activity, IL-13R alpha 1 plays a crucial role in mediating IL4 and IL13 responses. The interleukin-13 receptor complex comprises IL4R, IL13RA1, and potentially other components, illustrating the intricacies of its molecular architecture. Additionally, IL-13R alpha 1 interacts with TRAF3IP1 and IL4, contributing to its involvement in diverse signaling pathways and underscoring its significance as a component of the interleukin-13 receptor system.

Mouse

HEK293

C-Avi;C-6*His

O09030 (A25-T340)

16164  [NCBI]

Partial

Biotin

The single lysine residue in Avitag is biotinylated through an enzymatic reaction.

AATEVQPPVTNLSVSVENLCTIIWTWSPPEGASPNCTLRYFSHFDDQQDKKIAPETHRKEELPLDEKICLQVGSQCSANESEKPSPLVKKCISPPEGDPESAVTELKCIWHNLSYMKCSWLPGRNTSPDTHYTLYYWYSSLEKSRQCENIYREGQHIACSFKLTKVEPSFEHQNVQIMVKDNAGKIRPSCKIVSLTSYVKPDPPHIKHLLLKNGALLVQWKNPQNFRSRCLTYEVEVNNTQTDRHNILEVEEDKCQNSESDRNMEGTSCFQLPGVLADAVYTVRVRVKTNKLCFDDNKLWSDWSEAQSIGKEQNST

Approximately 58-85 kDa,based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.