Human IL-1ra/IL-1F3 Quantikine ELISA Kit Summary
Background |
The Quantikine Human IL-1ra Immunoassay is a 4.5 hour solid phase ELISA designed to measure IL-1ra in cell culture supernates, serum, and plasma. It contains E. coli-derived recombinant human IL-1ra as well as antibodies raised against the recombinant factor. This immunoassay has been shown to accurately quantitate recombinant human IL-1ra. Results obtained using natural human IL-1r...a showed linear curves that were parallel to the standard curves obtained using the Quantikine kit standards. These results indicate that this kit can be used to determine relative mass values for natural human IL-1ra. |
Specificity |
Natural and recombinant human IL-1ra |
Source |
N/A |
Inter-Assay |
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Intra-Assay |
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Spike Recovery |
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Sample Volume |
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Gene |
IL1RN |
Applications/Dilutions
Dilutions |
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Application Notes |
Interference observed with 1 or more available related molecules. |
Publications |
Read Publications using DRA00B in the following applications:
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Packaging, Storage & Formulations
Storage |
Store the unopened product at 2 - 8 °C. Do not use past expiration date. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Human IL-1ra/IL-1F3 Quantikine ELISA Kit
Background
Interleukin-1 receptor antagonist (IL-1ra; also known as
IL-1F3) is a 22-25 kDa member of the
IL-1 family of cytokines. Currently, there are 11 family
members (IL-1F1-F11), nine of which form
an IL-1 gene cluster on human Ch2 (1-3). Each IL-1 family
member contains an IL-1 fold. This
fold is generated by 12 packed beta -sheets that interact to
form a beta -trefoil structure. Little amino
acid (aa) homology is required to achieve this structure,
and this explains the low aa identity
among IL-1 family members. IL-1ra is a pure cytokine receptor
antagonist that has no signal
transduction-initiating activity (4). It is an acute phase
protein that exists to dampen
inflammation. IL-1( beta ) is initially produced by monocytes in
response to a variety of stimuli.
Circulating IL-1 then binds to widely expressed IL-1 type I
receptors (IL-1 RI) and initiates a
number of pro-inflammatory events. On endothelial cells
(EC), IL-1 induces PGE2 and IL-6
release, generating fever, thrombocytosis, and hepatic acute
phase protein production. In
synovial joints, IL-1 induces chondrocyte NO production, an
event that leads to reduced
collagen synthesis and chondrocyte apoptosis. Finally, IL-1
increases neutrophil counts, both in
blood and tissue, and thus is able to promote a
pro-inflammatory environment in multiple
locations (5-8). IL-1ra blocks IL-1 action through
competitive inhibition. More correctly,
although IL-1ra fills the IL-1 binding site in IL-1 RI, it
is also unable to orchestrate the creation of
a signal-transducing IL-1 RI:IL-1 R Accessory protein (IL-1
R AcP) heterodimer complex. Effective
IL-1ra concentrations are generally 100-fold greater than
local IL-1 concentrations. This is
because the IL-1ra half-life is but 6 minutes, and very few
IL-1 type I receptors need to be
engaged by IL-1 to elicit a cellular response (5, 7, 9).
Human IL-1ra is synthesized as a 177 aa precursor that
contains a 25 aa signal sequence and a
152 aa mature region (10, 11). Although it contains an IL-1
cytokine fold, it apparently lacks two
structural motifs that allow for activation of the IL-1
receptor heterodimer. First, and following
binding to IL-1 RI, the presence of Ile 51-His 54 and Lys
145 of the mature molecule preclude
recruitment of IL-1 R AcP. Second, there is no identifiable
C-terminal lectin segment that is
hypothesized to help recruit an accessory signaling
component (1, 12, 13). Mature human
IL-1ra is 77% and 82% aa identical to mouse and canine
IL-1ra, respectively, and human IL-1ra
inhibits IL-1 activity on mouse cells (10). A number of cell
types express IL-1ra, including
monocytes (11), Sertoli cells (14), hepatocytes (15),
adipocytes (16), synovial fibroblasts (17),
mast cells (18), pancreatic beta -cells (19), and intestinal
epithelial cells (20). There are at least three
intracellular IL-1ra isoforms (icIL-1ra1, 2, and 3). All
show N-terminal variation, and all contain
amino acids 35-177 of the secreted precursor (21-23).
Intracellular IL-1ra1 is of particular
interest, because it is reported to be "secreted"
by endothelial cells and binds to the IL-1 RI in
an antagonist fashion (23-25). Intracellular IL-1ra1 is 159
aa in length and shows a 3 aa
substitution for the first 21 aa's of the signal sequence of
IL-1ra (21).
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⚠ WARNING: This product can expose you to chemicals including N,N-Dimethylforamide, which is known to the State of California to cause cancer. For more information, go to www.P65Warnings.ca.gov.
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