Recombinant Mouse IFNG (E. coli)



DescriptionIFN-gamma is produced mainly by T-cells and natural killer cells activated by antigens, mitogens, or alloantigens. It is produced by lymphocytes expressing the surface antigens CD4 and CD8. IFN gamma receptors are expressed on all types of human cells with the exception of mature erythrocytes. IFN-gamma-receptor complexes are rapidly internalized by endocytosis. IFN-gamma has antiviral and antiparasitic activities and also inhibits the proliferation of a number of normal and transformed cells. Interferon-gamma synergises with TNF-alpha and TNF-beta in inhibiting the proliferation of various cell types. The growth inhibitory activities of IFN-gamma are more pronounced than those of the other interferons. However, the main biological activity of IFN-gamma appears to be immunomodulatory in contrast to the other interferons that are mainly antiviral. T helper cells IL-2 induces the synthesis of IFN-gamma and other cytokines. IFN-gamma acts synergistically with IL-1 and IL-2 and appears to be required for the expression of IL-2 receptors on the cell surface of T lymphocytes. Blocking of the IL-2 receptor by specific antibodies also inhibits the synthesis of IFN-gamma.
FamilyIL-10/Interferon Family
Recombinant Mouse Interferon-Gamma (IFNG)
Gene SymbolIFNG
Gene ID15978
Accession NumberP01580
SourceE. coli
SpeciesMouse (M. musculus)
AppearanceLyophilized Powder
Molecular Weight17 kDa
Endotoxin Level<1.0 EU/µg of recombinant protein as determined by the LAL method.
Purity>95% as determined by SDS-PAGE
FormulationRecombinant Interferon gamma was lyophilized from a 0.2μm filtered concentrated (1.0 mg/mL) solution in PBS, pH 7.2.
FunctionThe ED(50) was determined by a viral resistance assay of mouse L929 cells and was found to be ? 1.0 ng/mL, corresponding to a specific activity of ? 1.0 x 10^6 units/mg.
ReconstitutionA 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.
StorageThe 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 lo
UsageFor research use only. Not for diagnostic or therapeutic use.

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.

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