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Recombinant Mouse IL1A


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Product Source Size Cat. No. Price
Recombinant Mouse IL1A E. coli10 µg Z200095 $70.00
100 µg Z200097 $490.00
1.0 mg Z200099 $2,900.00
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Data Sheet
Print Version
Alternative Names IL-1 alpha, IL1a
Recombinant Mouse Interleukin-1 Alpha (IL1A)
Description Monocytes are the main source of secreted IL-1. They express predominantly IL-1- beta while human keratinocytes express large amounts of IL-1-alpha. Murine macrophages display a transition from IL-1-beta to IL-1-alpha production during maturation of monocytes into inflammatory macrophages. There are two functionally almost equivalent forms of IL-1, IL-1-alpha and IL-1-beta that are encoded by two different genes. IL-1-beta is the predominant form in humans while it is IL-1-alpha in mice. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The IL-1-beta but not the IL-1-alpha precursor must be processed before it can bind to the receptor. Both forms of IL-1 bind to the same receptor and therefore also show similar if not identical biological activities. The receptor isolated from T-cells is expressed predominantly on T cells and cells of mesenchymal origin. It binds both types of IL-1 with equal affinity. This type is called also Type 1 receptor. It has been designated CD121a. The Type 2 receptor has been designated CD121b. It is isolated from B-cells, granulocytes, and macrophages. It is expressed predominantly on B-cells and cells of the myelomonocytic lineage and is encoded by a separate gene.
Gene Symbol IL1A
Gene ID 16175
Accession No. P01582
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 18.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Gel Image Click To Enlarge
Bioactivity The ED(50) was determined by a cell proliferation assay using the murine helper T cell line, D10.G4., was found to be 10.0 pg/mL.
Bioactivity Data Click To Enlarge
Formulation Recombinant mouse Interleukin-1 alpha was lyophilized from a 0.2 μm filtered PBS solution.
Reconstitution A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
Submit a new question:
How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.