IL-1 alpha Protein, Human (HEK293)

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][4]. IL-1 alpha protein, Human (HEK293) is a recombinant protein consisting of 159 amino acids (S113-A271) and is produced by HEK293 cells.

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 inhibits differentiation of preadipocytes and lipid accumulation^[2]. IL-1 alpha induces apoptosis and inhibits the osteoblast differentiation^[3]. IL-1 alpha trigger inflammation in a pathway initiated through Myd88 activation and culminated in NF-κB–induced transcription of inflammatory genes^[4].

IL-1 alpha (human) (.1-1 ng/mL) increases the IL-1-beta mRNA levels in EC derived from adult human saphenous vein in a concentration- and time-dependent manner, and induces the release of biologically active IL-1 from endothelial cell (EC)^[6].
IL-1 alpha (human) (-1 ng/mL; 6h) stimulates prostaglandin E2 and bone resorption in a dose-dependent manner^[7].

IL-1 alpha (1 µg/kg; i.p.) significantly increases the TG (triglyceride) level at 12 h in serum in C57BL/6J male mice^[2].

1.Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells and the ED₅₀ is 3.904 pg/mL.
2. Measured by its ability to induced Interferon gamma secretion by human natural killer lymphoma NK-92 cells and the ED₅₀ is ≤0.35 μg/mL.

Human

HEK293

Tag Free

P01583/NP_000566.3 (S113-A271)

3552  [NCBI]

Approximately 19-23 kDa

Greater than 90% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris, 100 mM NaCl, pH 8.0 or PBS, pH 7.4, 8% trehalose. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. 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.

• [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]