IL-1R1 Protein, Human (HEK293)

IL-1R1 (CD121a) belongs to IL-1 receptor, and binds to IL-1α, IL-1β, IL-1Ra and IL-38 with comparable affinities (K_d: 0.1-1 nM)^[1]. IL-1R1 regulates the transcription of multiple proinflammatory cytokines and mediates immune and inflammatory responses, including the activation of NF-κB and MAPK pathway^[4]. I IL-1R1 Protein, Human (HEK293) is a recombinant human extracellular region of IL-1R1 (M1-T332) without any tag, which is produced in HEK293 cells.

IL-1R1 (CD121a), a member of IL-1 receptor, is a receptor for IL-1α, IL-1β, IL-1Ra and IL-38, thereby mediating IL-1-dependent activation^[1]. IL-1R1 is expressed in specific endothelial cells, ventricular cells, astrocytes, and neurons^[2].
The sequence of amino acids in IL-1R1 differs in different species. Human IL-1R1 shares <70% aa sequence identity with mouse and rats.
IL-1R1 binds to IL-1 by forming a heterodimer with IL-1R3 (IL-1RAcP). The heterodimer is responsible for the signal transduction by the hydrolysis of GTP, followed by JNK and p38 MAP kinase^[3]. Upon binding of IL-1, IL-1R1 initiates the downstream signaling cascade (MAPK p38 and NF-κB pathway)^[4]. IL-1R1 signaling induces human Th17 cell differentiation and commitment, which is crucial in the development of autoimmune diseases^[4].
IL-1R1 mediates immune and inflammatory responses. IL-1R1 mediates the activation of NF-κB, MAPK pathway.

Human IL-1 Beta, His Tag captured on CM5 Chip via Anti-his antibody can bind Human IL-1R1, No Tag with an affinity constant of 11.37 nM as determined in SPR assay (Biacore T200).

Human

HEK293

Tag Free

P14778/NP_000868.1 (L18-T332)

3554  [NCBI]

Extracellular Domain

LEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGIDAAYIQLIYPVT

Approximately 50-65 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

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

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Diana Boraschi, et al. The family of the interleukin-1 receptors. Immunol Rev. 2018 Jan;281(1):197-232.  [Content Brief]

  [2]. Daniel P Nemeth, et al. Modulation of Neural Networks by Interleukin-1. Brain Plast. 2021 Aug 23;7(1):17-32.  [Content Brief]

  [3]. Naoe Kaneko, et al. The role of interleukin-1 in general pathology. Inflamm Regen. 2019 Jun 6;39:12.  [Content Brief]

  [4]. Yonggang Sha, et al. A role of IL-1R1 signaling in the differentiation of Th17 cells and the development of autoimmune diseases. Self Nonself. 2011 Jan;2(1):35-42.  [Content Brief]