IL1A Human, His Active
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
Greater than 90% as determined by SDS-PAGE.
Description
IL1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (113-271 a.a) and having a molecular mass of 22.4kDa. IL1A is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
IL-1 alpha, produced by activated macrophages, is an important inflammatory mediator. This cytokine acts as an endogenous pyrogen, triggers the production of prostaglandin and collagenase from synovial cells, and plays a crucial role in immune cell activation. Specifically, IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, promotes B-cell maturation and proliferation, and enhances fibroblast growth factor activity.
Recombinant Human IL1A, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 197 amino acids (residues 113-271). This protein, with a molecular weight of 22.4 kDa, includes an N-terminal 38 amino acid His-tag and undergoes purification using proprietary chromatographic methods.
The IL1A protein solution is provided at a concentration of 1 mg/ml in a buffer containing 20mM Tris-HCl (pH 7.5) and 10% glycerol.
The addition of a carrier protein such as 0.1% HSA or BSA is advised for long-term storage.
Repeated freezing and thawing should be avoided.
The purity of IL1A is determined to be greater than 90% using SDS-PAGE analysis.
The biological activity of IL1A is assessed by its ability to stimulate the proliferation of D10.G4.1 mouse helper T cells. The ED50 for this effect, representing the concentration at which 50% of maximal proliferation is observed, is less than or equal to 0.04 ng/ml.
Interleukin-1 alpha, IL-1 alpha, Hematopoietin-1, Interleukin-1 alpha: Interleukin-1a, IL-1a, Interleukin-1 alpha, IL1A, interleukin 1 alpha, IL1F1, IL-1A, preinterleukin 1 alpha, pro-interleukin-1-alpha.
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA PFSFLSNVKY NFMRIIKYEF ILNDALNQSI IRANDQYLTA AALHNLDEAV KFDMGAYKSS KDDAKITVIL RISKTQLYVT AQDEDQPVLL KEMPEIPKTI TGSETNLLFF WETHGTKNYF TSVAHPNLFI ATKQDYWVCL AGGPPSITDF QILENQA.
Product Science Overview
Interleukin-1 alpha (IL-1α) is a proinflammatory cytokine that plays a crucial role in the regulation of immune responses. It is part of the interleukin-1 family and is encoded by the IL1A gene in humans . IL-1α is produced by a variety of cell types, including macrophages, neutrophils, epithelial cells, and endothelial cells .
The recombinant form of IL-1α, specifically the human recombinant with a His tag, is produced using various expression systems such as HEK293 cells or Escherichia coli . The His tag is a sequence of histidine residues added to the protein to facilitate purification through affinity chromatography. The recombinant IL-1α typically consists of a polypeptide chain containing 159 amino acids (from Ser113 to Ala271) and has a molecular mass of approximately 22.5 kDa .
IL-1α is known for its wide range of biological activities, including metabolic, physiological, and hematopoietic functions . It exerts its effects by binding to specific cell surface receptors, leading to the activation of various signaling pathways that promote inflammation, fever, and sepsis . The recombinant form of IL-1α retains these biological activities and is often used in research to study its effects and potential therapeutic applications.
Recombinant IL-1α is widely used in laboratory research to investigate its role in immune responses and its potential as a therapeutic target. It is utilized in various assays, including ELISA, Western blotting, immunofluorescence, and immunohistochemistry . The His tag allows for easy purification and detection of the protein in these assays.
The recombinant IL-1α protein is typically lyophilized and can be stored at -20°C to -80°C for long-term preservation . After reconstitution, the protein solution is stable at -20°C for up to three months and at 2-8°C for up to one week. To maintain its stability, it is recommended to add a carrier protein or stabilizer and to avoid repeated freeze-thaw cycles .
