IL1R2 Protein, Human, Recombinant (His Tag)

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IL1R2 Protein, Human, Recombinant (His Tag): Product Information

Purity
> 98 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
1. Measured by its ability to inhibit IL1β-dependent proliferation in D10.G4.1 mouse helper T cells.
The ED50 for this effect is typically 5.5 μg/mL in the presence of 40 pg/mL of rhIL1β.
2. Measured by its ability to inhibit Interferon gamma secretion by human natural killer lymphoma NK-92 cells in the presence of 500pg/mL IL1b.
The EC50 for this effect is typically 20-80ng/mL.
Protein Construction
A DNA sequence encoding the extracellular domain (Met 1-Glu 343) of human IL1R2 (NP_004624.1) was expressed, with a fused C-terminal polyhistidine tag.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Phe 14
Molecule Mass
The recombinant human IL1R2 consists of 342 amino acids and has a predicted molecular mass of 39.3 kDa. As a result of glycosylation, the rh IL1R2 migrates as an approximately 50-55 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

IL1R2 Protein, Human, Recombinant (His Tag): Images

IL1R2 Protein, Human, Recombinant (His Tag): Alternative Names

CD121b Protein, Human; CDw121b Protein, Human; IL-1R-2 Protein, Human; IL-1RT-2 Protein, Human; IL-1RT2 Protein, Human; IL1R2c Protein, Human; IL1RB Protein, Human

IL1R2 Background Information

Interleukin 1 receptor, type II (IL1R2) also known as CD121b (Cluster of Differentiation 121b) is a cytokine receptor that belongs to the interleukin-1 receptor family. This protein binds interleukin alpha (IL1A), interleukin beta (IL1B), and interleukin 1 receptor, type I (IL1R1/IL1RA), and acts as a decoy receptor that inhibits the activity of its ligands. The pleiotropic cytokine IL1 is produced to regulate development and maintenance of the inflammatory responses, and binds to specific plasma membrane receptors on cells. Two distinct types of IL1 receptors which are able to bind IL1 specifically have been identified, designated as IL1RI (IL1RA) and IL1RII (IL1RB). IL1R1 contributes to IL-1 signaling, whereas the IL-1R2/CD121b has no signaling property and acts as a decoy for IL-1. IL-1R2/CD121b structurally consisting of a ligand binding portion comprised of three Ig-like domains, a single transmembrane region, and a short cytoplasmic domain, is expressed in a variety of cell types including B lymphocytes, neutrophils, monocytes, large granular leukocytes and endothelial cells. Interleukin 4 (IL4) is reported to antagonize the activity of interleukin 1 by inducing the expression and release of this cytokine.
Full Name
interleukin 1 receptor, type II
References
  • Cannon JG, et al. (1997) Interleukin-1 beta, interleukin-1 receptor antagonist, and soluble interleukin-1 receptor type II secretion in chronic fatigue syndrome. J Clin Immunol. 17 (3): 253-61.
  • Liu C, et al. (1996) Cloning and characterization of an alternatively processed human type II interleukin-1 receptor mRNA. J Biol Chem. 271 (34): 20965-72.
  • Van der Poll T, et al. (1997) Antiinflammatory cytokine responses during clinical sepsis and experimental endotoxemia: sequential measurements of plasma soluble interleukin (IL)-1 receptor type II, IL-10, and IL-13. J Infect Dis. 175 (1): 118-22.
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