IL1A ELISA Kit

Catalog No. ABIN4986939

This Rat IL1A ELISA Kit is a Colorimetric ELISA Kit designed to quantify Rat IL1A.

Quick Overview for IL1A ELISA Kit (ABIN4986939)

Target: IL1A (Interleukin 1 alpha (IL1A))

Reactivity: Rat

Detection Method: Colorimetric

Method Type: Sandwich ELISA

Detection Range: 0.02-1.0 ng/mL

Application: ELISA

Sample Type: Cell Culture Supernatant, Serum, Plasma (heparin), Plasma (citrate), Plasma (EDTA)

Product Details IL1A ELISA Kit

Minimum Detection Limit: 0.02 ng/mL

Analytical Method: Quantitative

Specificity: Natural and recombinant Rat IL-1α Ligand

Sensitivity: 7 pg/mL

Material not included:

• Microplate reader.
• Pipettes and pipette tips.
• EP tube Deionized or distilled water.

Application Details

Application Notes: Detection Wavelength: 450 nm

Sample Volume: 20 μL

Assay Time: 3 h

Plate: Pre-coated

Restrictions: For Research Use only

Handling

Storage: 4 °C

Target Details for IL1A

Target: IL1A (Interleukin 1 alpha (IL1A))

Alternative Name: IL-1alpha

Background: Interleukin-1α (IL-1α, also known as IL-1F1) and IL-1β (IL-1F2) are pleiotropic cytokines that belong to the IL-1 gene family. IL-1α and IL-1β bind to the same cell surface receptors and share biological functions. The two proteins have approximately 23 % amino acid (aa) sequence homology and both are synthesized as 31 kDa precursors that lack hydrophobic signal peptide sequences. Current evidence suggests that IL-1 proteins may be secreted via non-classical pathways (1-4).Rat IL-1α cDNA encodes a 270 aa residue pro-IL-1α precursor (5). The 114 aa pro-region contains a nuclear localization sequence, a lysine-based myristoylation site, one phosphorylation site, and one potential N-linked glycosylation site (5-8). The 156 aa mature region contains no cysteines and one potential N-linked glycosylation site (5). Pro-IL-1α is primarily localized to the cytosol after synthesis. It is known to translocate to the nucleus after cell activation and initiate gene transcription (9, 10). Some IL-1α is released extracellularly and exists as either a membrane-bound form or as a circulating 17 kDa molecule. When membranebound, membrane association is mediated either via a poorly-understood cell surface lectin interaction with the glycosylated IL-1α pro-form, or by interaction of myristoylated pro-IL-1α with plasma membrane phospho-lipids (8, 11-13). When released as a 17 kDa soluble form, calpain initiates cleavage of the pro-IL-1α precursor (14). Unlike pro-IL-1β, which is biologically inactive, both pro-IL-1α and mature IL-1α have been shown to be biologically active (15, 16). Within the mature protein, rat IL-1α shares 79 %, 60 %, 59 %, 58 %, 57 %, and 56 % aa sequence identity with mouse, rabbit, human, bovine, canine and feline proteins, respectively (17-21). Mammalian cells known to express IL-1α include brown adipocytes (22), keratinocytes (23), monocytes (24), macrophages (25), endothelial and smooth muscle cells (26), mast cells (27), Schwann cells (28), as well as osteoblasts and osteoclasts (29).Three type I transmembrane immunoglobulin superfamily proteins, IL-1 receptor type I (IL-1 R1), IL-1 receptor type II (IL-1 R2), and IL-1 receptor accessory protein (IL-1 RAcP, IL-1 R3)are involved in the formation of high affinity cell surface IL-1 receptor complexes. Both IL-1 R1 and IL-1 R2 can bind directly to IL-1α. IL-1 RAcP does not bind IL-1α directly, but interacts with IL-1 R1 in the presence of IL-1 to form the high-affinity receptor complex which is required for intracellular signal transduction. IL-1 RAcP also interacts with IL-1 R2 to form a non-functional high-affinity receptor complex that does not transduce IL-1 signals. Therefore, IL-1 R2 functions as a decoy receptor that attenuates IL-1α functions (16, 30, 31).IL-1α possesses a wide variety of biological activities and plays a central role in mediating immune and inflammatory responses. Normal production of IL-1α is critical for hematopoiesis, angiogenesis, osteoclast differentiation, and initiation of normal host responses to injury and infection(15,32-34). Inappropriate production of IL-1α has been implicated in the production of a variety of pathological conditions including sepsis, rheumatoid arthritis, inflammatory bowel disease, insulin-dependent diabetes mellitus, and atherosclerosis (1, 13, 15).

Pathways: NF-kappaB Signaling, Autophagy, Cancer Immune Checkpoints