IL-1 alpha Protein, Mouse
Based on 2 publication(s) in Google Scholar
IL-1 alpha is a ubiquitous and pivotal pro-inflammatory cytokine. IL-1 alpha is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha plays an important role in inflammation and bridges the innate and adaptive immune systems. IL-1 alpha mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. IL-1 alpha protein, Mouse is a recombinant protein consisting of 156 amino acids (S115-A270) and is produced by E. coli.
- Species: Mouse
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
IL-1 alpha is a ubiquitous and pivotal pro-inflammatory cytokine. IL-1 alpha is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha plays an important role in inflammation and bridges the innate and adaptive immune systems. IL-1 alpha mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways[1][2]. IL-1 alpha protein, Mouse is a recombinant protein consisting of 156 amino acids (S115-A270) and is produced by E. coli.
IL-1 alpha (interleukin-1 alpha) is a major agonist of IL-1. IL-1α is present in all mesenchymal cells in particular, cells rich in IL-1α constitute tissues with a barrier function, such as keratinocytes in the skin, type 2 epithelial cells in the lung, the epithelium of the entire gastrointestinal tract, endothelial cells in blood vessels, and astrocytes in the brain[1]. The precursor of IL-1α (ProIL-1α) is processed by the Ca2+-dependent protease calpain (including caspase-1) into the mature 17 kDa form and the 16 kDa N-terminal cleavage product – the propiece of IL-1α, also termed IL-1α N-terminal peptide (IL-1NTP). The latent form of calpain is activated in cells under inflammatory conditions and especially upon loss of plasma membrane integrity, which occurs during necrosis. pro-IL-1α and mature IL-1α bind to IL-1R and induces the secretion of IL-6 and TNF[5]. IL-1α acts as an ‘alarmin’ and as a primum movens of tissue inflammation[1]. IL-1 alpha trigger inflammation in a pathway initiated through Myd88 activation and culminated in NF-κB–induced transcription of inflammatory genes[2]. IL-1 alpha inhibits differentiation of preadipocytes and lipid accumulation[3]. IL-1 alpha induces apoptosis and inhibits the osteoblast differentiation[4].
IL-1 alpha (0.5, 1, 2.5, 5, 10 ng/mL; 5 days) significantly reduces the cell viability in MC3T3-E1 cells[4].
IL-1 alpha (0.5, 1, 2.5, 5, 10 ng/mL 24 h) decreases the ALP and caspase-3 activity in MC3T3-E1 cells, increases the expression of Bax and caspase-3 mRNA and protein level in a dose-dependent manner, decreases the mRNA expression and the protein levels of Runx2, ALP, OSX and OCN; induces apoptosis[4].
IL-1 alpha (10 µg/kg; i.p.) significantly increases the TG (triglyceride) level at 12 h in serum in C57BL/6J male mice[3].
IL-1 alpha (1, 10, 100 ng/mL; 8 days) inhibits differentiation of preadipocytes and lipid accumulation in a dose-dependent manner in 3T3-L1 cells[3].
1. The ED50 is <2 pg/mL as measured by murine D10S cells, corresponding to a specific activity of >5.0 × 108 units/mg.
2. Measured in a proliferation assay using CTLL-2 Mouse T lymphocytes cell. The ED50 for this effect is 0.5597 pg/mL, corresponding to a specific activity is 1.787×109 units/mg.
3. Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 for this effect is 0.935 pg/mL, corresponding to a specific activity is 1.07×109 units/mg.
Publications (2)
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Journal Impact Factor
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Most Recent
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J Adv Res
Tocilizumab-loaded nanoparticles block IL-6R and reduce edema after intracerebral hemorrhage. [Abstract]2026 Feb 16:S2090-1232(26)00158-X. PMID: 41707962 -
Int J Biol Macromol
Astrocyte-conditional knockout of MOB2 inhibits the phenotypic conversion of reactive astrocytes from A1 to A2 following spinal cord injury in mice. [Abstract]2025 Apr:300:140289. PMID: 39863205
Technical Parameters
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Species Mouse
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Source E. coli
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Tag Tag Free
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Accession
P01582 (S115-S270)
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Molecular Construction
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N-term
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IL-1α (S115-S270)
Accession # P01582 -
C-term
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Protein Length
Full Length of Mature Protein
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Synonyms
IL1A; IL-1A; Prev. IL1; Preinterleukin 1 Alpha; IL1F1; Interleukin-1 Alpha; Hematopoietin-1; IL-1 Alpha; IL1-ALPHA; Interleukin 1 Alpha; Pro-Interleukin-1-Alpha
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AA Sequence
SAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS
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Predicted Molecular Mass
18 kDa
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Molecular Weight
Approximately 16 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 6% sucrose, 2% mannitol, 50 mM Arginine, 0.03% Tween 80, pH 8.0.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
3.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[1]. Cavalli G, et al. Interleukin 1α: a comprehensive review on the role of IL-1α in the pathogenesis and treatment of autoimmune and inflammatory diseases. Autoimmun Rev. 2021 Mar;20(3):102763. [Content Brief]
[2]. Wu T, et al. Involvement of p38 and p42/44 MAP kinases and protein kinase C in the interferon-gamma and interleukin-1alpha-induced phosphorylation of 85-kDa cytosolic phospholipase A(2) in primary human bronchial epithelial cells. Cytokine. 2004 Jan 7;25(1):11-20. [Content Brief]
[3]. Um JY, et al. Functional polymorphism of IL-1 alpha and its potential role in obesity in humans and mice. PLoS One. 2011;6(12):e29524. [Content Brief]
[4]. Guo C, et al. IL-1α induces apoptosis and inhibits the osteoblast differentiation of MC3T3-E1 cells through the JNK and p38 MAPK pathways. Int J Mol Med. 2016 Jul;38(1):319-27. [Content Brief]
[5]. Malik A,et al. Function and regulation of IL-1α in inflammatory diseases and cancer. Immunol Rev. 2018 Jan;281(1):124-137. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)