IL1R1 Protein, Rat, Recombinant (His & Fc Tag)

1/1
Price:
Size:
Number:

IL1R1 Protein, Rat, Recombinant (His & Fc Tag): Product Information

Purity
> 85 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured by its ability to inhibit IL1α-dependent proliferation in D10.G4.1 mouse helper T cells(Symons, J.A. et al. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 272.).
The ED50 for this effect is typically 5-20 μg/ml in the presence of 40 pg/mL of recombinant human IL1a.
Protein Construction
A DNA sequence encoding the rat IL1R1 (NP_037255.3) extracellular domain (Met 1-Lys 352) was was fused with the C-terminal His-tagged Fc region of mouse IgG1 at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Rat
Predicted N Terminal
Leu 34
Molecule Mass
The recombinant rat IL1R1/mFc is a disulfide-linked homodimer. The reduced monomer comprises 562 amino acids and predicts a molecular mass of 64.6 kDa. The apparent molecular mass of the ratIL1R1/mFc monomer is approximately 90-95 kDa in SDS-PAGE under reducing conditions due to glycosylation.
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 -20℃ to -80℃
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.

IL1R1 Protein, Rat, Recombinant (His & Fc Tag): Images

IL1R1 Background Information

Interleukin 1 receptor, type I (IL-1R1) also known as CD121a (Cluster of Differentiation 121a), is an interleukin receptor. IL-1R1/CD121a is a cytokine receptor that belongs to the interleukin 1 receptor family. This protein is a receptor for interleukin alpha (IL1A), interleukin beta (IL1B), and interleukin 1 receptor, type I (IL1R1/IL1RA). IL-1R1/CD121a is an important mediator involved in many cytokine induced immune and inflammatory responses. This protein has been characterized by pharmacological and molecular techniques in the mouse brain. The spindle-shaped astrocytes enclose the wound, separating the healthy from damaged neural tissue. The shape change and subsequent repair processes are IL-1β activity-dependent, acting through the IL-1 type 1 receptor (IL-1R1), as co-application of the IL-1type 1 receptor antagonist protein (IL-1ra) blocks IL-1β induced effects. In the spleen, a slight increase in IL-1R AcP and IL-1R1 was observed during the first hours following LPS stimulation. In conclusion, IL-1R AcP mRNA is expressed in the brain and in other tissues where IL-1R1/CD121a transcripts are found. However, the regulation of its expression is distinct from IL-1R1/CD121a. The high level of expression and the lack of regulation of IL-1R AcP transcripts in the brain under inflammatory conditions suggest that the protein might be constitutively expressed in excess.
Full Name
interleukin 1 receptor, type I
References
  • Dale M, et al. (1999). "Interleukin-1 receptor cluster: gene organization of IL1R2, IL1R1, IL1RL2 (IL-1Rrp2), IL1RL1 (T1/ST2), and IL18R1 (IL-1Rrp) on human chromosome 2q.". Genomics 57 (1): 177-9.
  • Joos L, et al. (2001). "Association of IL-1beta and IL-1 receptor antagonist haplotypes with rate of decline in lung function in smokers.". Thorax 56 (11): 863-6.
  • Vigers GP, et al. (1997). "Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta.". Nature 386 (6621): 190-4.
Add to Cart Successfully Add to Cart Failed Shopping cart is being updated, please wait