Typical Testing Data/Standard Curve (for reference only)
Human IL-1 alpha ELISA Kit | IL-1alpha elisa kit
Human IL-1 alpha ELISA Kit
Gene Names
IL1A; IL1; IL-1A; IL1F1; IL1-ALPHA
Reactivity
Human
Synonyms
IL-1 alpha; Human IL-1 alpha ELISA Kit; IL-1alpha elisa kit
Reactivity
Human
Sequence Length
271
Samples
Cell culture supernate, serum and plasma
Assay Type
Quantitative Sandwich
Preparation and Storage
Store at 4 degree C.
Typical Testing Data/Standard Curve (for reference only)
Typical Testing Data/Standard Curve (for reference only)
Related Product Information for IL-1alpha elisa kit
Principle of the Assay: This assay employs the quantitative sandwich enzyme immunoassay technique. A monoclonal antibody specific for IL-1alpha has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any IL-1alpha present is bound by the immobilized antibody. Following incubation unbound samples are removed during a wash step, and then a detection antibody specific for IL-1alpha is added to the wells and binds to the combination of capture antibody-IL-1alpha in sample. Following a wash to remove any unbound combination, and enzyme conjugate is added to the wells. Following incubation and wash steps, a substrate is added. A colored product TMB is formed in proportion to the amount of IL- 1alpha present in the sample. The reaction is terminated by addition of acid and absorbance is measured. A standard curve is prepared from seven IL-1alpha standard dilutions and IL-1alpha sample concentration determined.
Background/Introduction: Interleukin 1 (IL-1) is a name that designates two proteins, IL-1alpha and IL-1beta, which are the products of distinct genes, but which recognize the same cell surface receptors. With the exception of skin keratinocytes, some epithelial cells, and certain cells of the central nervous system, IL-1 is not produced by the cells of healthy individuals. However, in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins, a dramatic increase in the production of IL-1 by macrophages and various other cell types is seen. For reviews on the properties and activities of IL-1alpha and IL-1beta, see references 1-3. IL-1alpha and IL-1beta are structurally related polypeptides that show approximately 25% homology at the amino acid (aa) level (2). Both are synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17.5 kDa (4, 5). Neither IL-1alpha nor IL-1beta contains a typical hydrophobic signal peptide sequence (6-8), but evidence suggests that these factors can be secreted by non-classical pathways (9, 10). A large proportion of IL-1alpha is retained intracellularly in its precursor form (3). A portion of this unprocessed IL-1alpha is transported to the cell surface and remains associated with the cell membrane (1, 3, 11). The membrane-bound, unprocessed IL-1alpha is apparently biologically active, acting in a paracrine fashion on adjacent cells having IL-1 receptors (1, 3). The precursor form of IL-1beta, unlike the IL-1alpha precursor, shows little or no biological activity in comparison to the 17.5 kDa processed form (10-13). Intracellular IL-1beta consists exclusively of the 31 kDa precursor form (5). Extracellular IL-1beta consists of a mixture of both unprocessed and mature IL- 1beta. These results indicate that processing takes place subsequent to secretion and is not tightly coupled to secretion (5, 9, 10, 14). The specific protease apparently responsible for the processing of IL-1beta, designated interleukin1beta-converting enzyme (ICE), has been described (14). IL-1alpha and IL-1beta exert their effects by binding to specific receptors. Two distinct receptor types have been isolated that bind both forms of IL-1. An 80 kDa membrane bound receptor protein, IL-1 receptor type I (IL-1 RI), has been isolated from T cells, fibroblasts, keratinocytes, endothelial cells, synovial lining cells, chondrocytes, and hepatocytes (1, 3, 15). IL-1 RI has been cloned from mouse and human cells (16) and found to be a member of the Ig super family. A second type of IL-1 receptor, IL-1 receptor type II (IL-1 RII), has been found on B cells, neutrophils, and bone marrow cells (1, 3). This receptor has an apparent molecular weight of about 68 kDa and is also a member of the Ig super family. The two IL-1 receptor types show approximately 28% homology in their extracellular domains, but differ significantly in that the type II receptor has a cytoplasmic domain of only 29 aa residues, whereas the type I receptor has a cytoplasmic domain of 213 aa residues (1, 16). In general, IL-1alpha binds better to the type I receptor and IL-1beta binds better to the type II receptor (1).
Background/Introduction: Interleukin 1 (IL-1) is a name that designates two proteins, IL-1alpha and IL-1beta, which are the products of distinct genes, but which recognize the same cell surface receptors. With the exception of skin keratinocytes, some epithelial cells, and certain cells of the central nervous system, IL-1 is not produced by the cells of healthy individuals. However, in response to stimuli such as those produced by inflammatory agents, infections, or microbial endotoxins, a dramatic increase in the production of IL-1 by macrophages and various other cell types is seen. For reviews on the properties and activities of IL-1alpha and IL-1beta, see references 1-3. IL-1alpha and IL-1beta are structurally related polypeptides that show approximately 25% homology at the amino acid (aa) level (2). Both are synthesized as 31 kDa precursors that are subsequently cleaved into proteins with molecular weights of approximately 17.5 kDa (4, 5). Neither IL-1alpha nor IL-1beta contains a typical hydrophobic signal peptide sequence (6-8), but evidence suggests that these factors can be secreted by non-classical pathways (9, 10). A large proportion of IL-1alpha is retained intracellularly in its precursor form (3). A portion of this unprocessed IL-1alpha is transported to the cell surface and remains associated with the cell membrane (1, 3, 11). The membrane-bound, unprocessed IL-1alpha is apparently biologically active, acting in a paracrine fashion on adjacent cells having IL-1 receptors (1, 3). The precursor form of IL-1beta, unlike the IL-1alpha precursor, shows little or no biological activity in comparison to the 17.5 kDa processed form (10-13). Intracellular IL-1beta consists exclusively of the 31 kDa precursor form (5). Extracellular IL-1beta consists of a mixture of both unprocessed and mature IL- 1beta. These results indicate that processing takes place subsequent to secretion and is not tightly coupled to secretion (5, 9, 10, 14). The specific protease apparently responsible for the processing of IL-1beta, designated interleukin1beta-converting enzyme (ICE), has been described (14). IL-1alpha and IL-1beta exert their effects by binding to specific receptors. Two distinct receptor types have been isolated that bind both forms of IL-1. An 80 kDa membrane bound receptor protein, IL-1 receptor type I (IL-1 RI), has been isolated from T cells, fibroblasts, keratinocytes, endothelial cells, synovial lining cells, chondrocytes, and hepatocytes (1, 3, 15). IL-1 RI has been cloned from mouse and human cells (16) and found to be a member of the Ig super family. A second type of IL-1 receptor, IL-1 receptor type II (IL-1 RII), has been found on B cells, neutrophils, and bone marrow cells (1, 3). This receptor has an apparent molecular weight of about 68 kDa and is also a member of the Ig super family. The two IL-1 receptor types show approximately 28% homology in their extracellular domains, but differ significantly in that the type II receptor has a cytoplasmic domain of only 29 aa residues, whereas the type I receptor has a cytoplasmic domain of 213 aa residues (1, 16). In general, IL-1alpha binds better to the type I receptor and IL-1beta binds better to the type II receptor (1).
NCBI and Uniprot Product Information
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
Molecular Weight
30,607 Da
NCBI Official Full Name
interleukin-1 alpha
NCBI Official Synonym Full Names
interleukin 1 alpha
NCBI Official Symbol
IL1A
NCBI Official Synonym Symbols
IL1; IL-1A; IL1F1; IL1-ALPHA
NCBI Protein Information
interleukin-1 alpha
UniProt Protein Name
Interleukin-1 alpha
UniProt Gene Name
IL1A
UniProt Synonym Gene Names
IL1F1; IL-1 alpha
NCBI Description
The protein encoded by this gene is a member of the interleukin 1 cytokine family. This cytokine is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. This cytokine is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. This gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. It has been suggested that the polymorphism of these genes is associated with rheumatoid arthritis and Alzheimer's disease. [provided by RefSeq, Jul 2008]
Uniprot Description
Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Research Articles on IL-1alpha
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Product Notes
The Human IL-1alpha il1a (Catalog #AAA9135751) is an ELISA Kit and is intended for research purposes only. The product is available for immediate purchase. The AAA9135751 ELISA Kit recognizes Human IL-1alpha. It is sometimes possible for the material contained within the vial of "IL-1 alpha, ELISA Kit" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
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Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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