SRP3084
IL-1Ra human
recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture
Synonym(s):
ICIL-1RA, IL-1RN, IRAP
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About This Item
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
lyophilized
Assay:
≥98% (HPLC), ≥98% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
17.2 kDa
biological source
human
recombinant
expressed in E. coli
assay
≥98% (HPLC), ≥98% (SDS-PAGE)
form
lyophilized
potency
20-40 ng/mL
mol wt
17.2 kDa
packaging
pkg of 100 μg
technique(s)
cell culture | mammalian: suitable
impurities
<0.1 EU/μg endotoxin, tested
color
white to off-white
suitability
suitable for molecular biology
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... IL1R1(3554)
General description
Research Area: IMMUNO AND CKS
The interleukin-1 receptor antagonist (IL-1Ra) is part of the IL-1 family and binds to IL-1 receptors without triggering any intracellular response. IL-1Ra, produced by hepatic cells, exhibits characteristics of an acute phase protein. Endogenous IL-1Ra is generated in various experimental animal models of disease, as well as in human autoimmune and chronic inflammatory conditions.
The interleukin-1 receptor antagonist (IL-1Ra) is part of the IL-1 family and binds to IL-1 receptors without triggering any intracellular response. IL-1Ra, produced by hepatic cells, exhibits characteristics of an acute phase protein. Endogenous IL-1Ra is generated in various experimental animal models of disease, as well as in human autoimmune and chronic inflammatory conditions.
The gene IL-1RA (interleukin-1 receptor antagonist) is mapped to human chromosome 2q. It belongs to the IL-1 (interleukin 1) family of proteins. The encoded protein has a TIR (Toll/IL-1 receptor) domain. IL-1RA is produced by corneal epithelial cells, monocytes, neutrophils, macrophages and fibroblasts. It is a naturally occurring inflammatory inhibitor protein. Recombinant human IL-1RA is a 17.2kDa protein consisting of 153 amino acid residues.
Application
IL-1Ra human has been used as an IL1 antagonist to block the signaling from the IL1 receptor and verify that IL1 signaling is responsible for invasiveness in CD133-expressing cells. It has also been used as a control in sandwich enzyme-linked immunosorbent assay (ELISA) to measure protein levels.
Biochem/physiol Actions
Interleukin-1 receptor antagonist (IL-1RA) inhibits the activity of IL-1α (interleukin 1 α) and IL-1β (interleukin 1 β) by competitively blocking binding to their type I and type II receptors. Therapeutically, IL-1RA may help in the treatment of sepsis, rheumatoid arthritis, chronic myelogenous leukemia, asthma, psoriasis, and inflammatory bowel disease. Low production of IL-1RA is observed in HIV-1 (human immunodeficiency virus 1)-infected dendritic cells.
The interleukin-1 receptor antagonist (IL-1Ra) functions as a specific and selective competitive inhibitor of IL-1R1, binding to the receptor with high affinity.
Physical form
Lyophilized from 5mM Tris, pH 8.0 + 25 mM NaCl.
Preparation Note
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
Other Notes
MRPSGRKSSK MQAFRIWDVN QKTFYLRNNQ LVAGYLQGPN VNLEEKIDVV PIEPHALFLG IHGGKMCLSC VKSGDETRLQ LEAVNITDLS ENRKQDKRFA FIRSDSGPTT SFESAACPGW FLCTAMEADQ PVSLTNMPDE GVMVTKFYFQ EDE
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Association between interleukin-1 receptor antagonist (IL-1ra) gene polymorphism and early and late-onset psoriasis.
Tarlow JK
British Journal of Dermatology, 136, 147-148 (1997)
The molecular basis of nonoxynol-9-induced vaginal inflammation and its possible relevance to human immunodeficiency virus type 1 transmission.
The Journal of Infectious Diseases, 184, 418-428 (2001)
Therapies negating neuroinflammation after brain trauma
Hellewell S, et al.
Brain Research, 36-56 (2016)
Identification of critical regions within the TIR domain of IL-1 receptor type I.
Radons J
The International Journal of Biochemistry & Cell Biology, 68, 15-20 (2015)
The effects of interleukin-10 on interleukin-1 receptor antagonist and interleukin-1 beta production in human monocytes and neutrophils.
Jenkins JK
Lymphokine and Cytokine Research, 13, 47-54 (1994)
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