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Recombinant Human TNF

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Product Source Size Cat. No. Price
Recombinant Human TNF E. coli50 µg Z100855 $70.00
100 µg Z100857 $110.00
1.0 mg Z100859 $525.00
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Data Sheet
Print Version
Alternative Names TNFSF2, Cachectin, Differentiation-inducing factor (DIF), Necrosin, Cytotoxin
Recombinant Human Tumor Necrosis Factor Alpha (TNF)
Description Tumor Necrosis Factor is secreted by macrophages, monocytes, neutrophils, T cells, natural killer cells following their stimulation by bacterial lipopolysaccharides although cells expressing CD8(+) secrete little or no TNF-alpha. In addition, TNF is secreted by peripheral neutrophilic granulocytes and by a number of transformed cell lines that include those of astrocytes, microglial cells, smooth muscle cells and fibroblasts. Human milk also contains this factor. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL2, GM-CSF, SP, Bradykinin, Immune complexes, inhibitors of cyclooxygenase and platelet activating factor. TNF-alpha shares approximately 30% homology with TNF-beta. Human TNF-alpha is a non-glycosylated protein of 17.6 kDa.
Gene Symbol TNF
Gene ID 7124
Accession No. P01375
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 17.6 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 ED50 as determined by dose dependent proliferation of IL4 stimulated human megakaryocytic cell line was found to be ≤0.5 ng/mL
Bioactivity Data Click To Enlarge
Formulation Lyophilized from a 0.2 μm filtered solution in PBS (pH 7.2)
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
FAQs
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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.
Are there any tags in this product?
This product will not contain any conventional tags. However, it does have 4 extra amino acids that demarcate the start of the N-term (Glycine-Threonine-Alanine-Serine).