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IL1R1 antibody (Interleukin 1 Receptor, Type I)

Details for Product anti-IL1R1 Antibody No. ABIN116871, Supplier: Log in to see
Antigen
  • CD121A
  • D2S1473
  • IL-1R-alpha
  • IL1R
  • IL1RA
  • P80
  • CD121a
  • CD121b
  • IL-iR
  • Il1r-1
  • interleukin 1 receptor, type I
  • IL1R1
  • Il1r1
Alternatives
anti-Human IL1R1 antibody for Enzyme Immunoassay
Reactivity
Human
115
74
26
2
2
1
1
1
1
1
Host
Rabbit
115
33
26
19
2
1
Clonality
Polyclonal
Conjugate
This IL1R1 antibody is un-conjugated
13
11
9
8
5
5
1
1
1
1
Application
Enzyme Immunoassay (EIA), Immunoprecipitation (IP)
133
110
59
42
30
15
10
8
7
6
4
4
4
2
2
2
2
2
2
1
1
1
1
Options
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Immunogen The whole rabbit serum was prepared by repeated immunizations with recombinant human IL-1R type I.
Specificity This antiserum has been heated to 56 °C for 30 minutes. The antiserum is directed against the extracellular domain of the human IL-1R type I, but precipitates the intact receptor expressed on human cells. In general, this antibody also detects primate IL-1RI. The antibody does not recognize human IL-1, IL-1Ra or IL-1R type II. In ELISA formats and other immunoreactive assays, this antibody will detect the extracellular domain of the IL-1R type I (also called soluble IL-1R type I or "decoy" receptor) found in human body fluids, particularly in the circulation, urine and supernatants of cells and synovial fluid.
Purification Serum
Alternative Name CD121a / IL1R1 (IL1R1 Antibody Abstract)
Background IL1 binds antigen CD121a, which is a transmembrane glycoprotein and a member of the immunoglobulin superfamily expressed on T cells, thymocytes, dendritic cells, fibroblasts, vascular endothelial cells, epithelial cells and neural cells. CD121a binds the mature forms of IL1 alpha, IL1 beta, and IL1 Ra proteins. High affinity binding and signalling by the type I IL1 receptor requires CD121a and the accessory protein, IL1 R AcP, which does not bind IL1 alone, but forms a dimer capable of binding IL1. Interleukin 1 (IL1), which has a role as a mediator in inflammation, consists of 2 separate but related proteins, IL1 alpha and IL1 beta. Cell surface receptors for the 2 forms of IL1 are identical. IL1R Type I contains a single membrane spanning segment, a large cytoplasmic region, and an extracellular, IL1 binding portion composed of 3 immunoglobulin like domains.Synonyms: IL-1R-alpha, IL1R, IL1RA, IL1RT1, Interleukin-1 receptor alpha, Interleukin-1 receptor type 1, Interleukin-1 receptor type I
Gene ID 3554
NCBI Accession NP_000868
UniProt P14778
Research Area CD Antigens, Surface Receptors of Immune Cells
Pathways NF-kappaB Signaling, Carbohydrate Homeostasis
Application Notes This antiserum against anti-Human IL-1 Receptor Type I (IL-1RI) has been tested for use inELISA, Radioimmunoassays and Immunoprecipitation. Reactivity in other immunoassays isunknown. Recommended Dilutions: This product has been assayed for the ability toimmunoprecipitate antigen. A dilution range of 1: 400 to 1: 800 is suggested for thisimmunoassay. For immunoprecipitation, pre-clearing with a non-specific rabbit IgG ishelpful to reduce background. This product has been assayed by ELISA against soluble(extracellular) IL-1RI using HRP Conjugated Anti-Rabbit IgG [H&L] (Goat) (R1364HRP) andABTS as a substrate for 30 minutes at room temperature. A working dilution range of1: 1,000 to 1: 2000 is suggested for this product. This product has been assayed byradioimmunoassay against antigen. A dilution of 1: 8,000 is suggested for thisimmunoassay.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 85 mg/mL (by Refractometry)
Handling Advice Avoid repeated freezing and thawing.
Storage 4 °C/-20 °C
Storage Comment Store lyophilized product at 2-8 °C. Store the reconstituted antibody at 2-8 °C for one month (add 0.09% Sodium Azide) or at -20 °C for longer.
Background publications Schreuder, Tardif, Trump-Kallmeyer, Soffientini, Sarubbi, Akeson, Bowlin, Yanofsky, Barrett: "A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist." in: Nature, Vol. 386, Issue 6621, pp. 194-200, 1997 (PubMed).

Pruitt, Welborn, Edwards, Harward, Seeger, Martin, Smith, Kenney, Wesdorp, Meijer, Cuesta, Abouhanze, Copeland, Giri, Sims, Moldawer, Oldenburg: "Increased soluble interleukin-1 type II receptor concentrations in postoperative patients and in patients with sepsis syndrome." in: Blood, Vol. 87, Issue 8, pp. 3282-8, 1996 (PubMed).

Colotta, Dower, Sims, Mantovani: "The type II 'decoy' receptor: a novel regulatory pathway for interleukin 1." in: Immunology today, Vol. 15, Issue 12, pp. 562-6, 1995 (PubMed).

Arend, Malyak, Smith, Whisenand, Slack, Sims, Giri, Dower: "Binding of IL-1 alpha, IL-1 beta, and IL-1 receptor antagonist by soluble IL-1 receptors and levels of soluble IL-1 receptors in synovial fluids." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 153, Issue 10, pp. 4766-74, 1994 (PubMed).

Vigers, Caffes, Evans, Thompson, Eisenberg, Brandhuber: "X-ray structure of interleukin-1 receptor antagonist at 2.0-A resolution." in: The Journal of biological chemistry, Vol. 269, Issue 17, pp. 12874-9, 1994 (PubMed).

Colotta, Re, Muzio, Bertini, Polentarutti, Sironi, Giri, Dower, Sims, Mantovani: "Interleukin-1 type II receptor: a decoy target for IL-1 that is regulated by IL-4." in: Science (New York, N.Y.), Vol. 261, Issue 5120, pp. 472-5, 1993 (PubMed).

Mann, Micouin, Chiannilkulchai, Treich, Buhler, Sentenac: "RPC53 encodes a subunit of Saccharomyces cerevisiae RNA polymerase C (III) whose inactivation leads to a predominantly G1 arrest." in: Molecular and cellular biology, Vol. 12, Issue 10, pp. 4314-26, 1992 (PubMed).

McMahan, Slack, Mosley, Cosman, Lupton, Brunton, Grubin, Wignall, Jenkins, Brannan: "A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types." in: The EMBO journal, Vol. 10, Issue 10, pp. 2821-32, 1991 (PubMed).

Zagorski, Tollervey, Fournier: "Characterization of an SNR gene locus in Saccharomyces cerevisiae that specifies both dispensible and essential small nuclear RNAs." in: Molecular and cellular biology, Vol. 8, Issue 8, pp. 3282-90, 1989 (PubMed).

Dower, Wignall, Schooley, McMahan, Jackson, Prickett, Lupton, Cosman, Sims: "Retention of ligand binding activity by the extracellular domain of the IL-1 receptor." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 142, Issue 12, pp. 4314-20, 1989 (PubMed).