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Recombinant Human IL3

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Product Source Size Cat. No. Price
Recombinant Human IL3 E. coli10 µg Z100515 $70.00
50 µg Z100517 $130.00
1.0 mg Z100519 $1,890.00
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Data Sheet
Print Version
Alternative Names IL-3, Mast cell growth factor, MCGF, Multi-CSF, Hematopoietic growth factor, HCGF, P-cell stimulation factor
Recombinant Human Interleukin-3 (IL3)
Description IL3 is produced mainly by T cells following cell activation by antigens and mitogens, but also by keratinocytes, natural killer cells, mast cells, endothelial cells, and monocytes. The analysis of bacterial- derived recombinant IL3 shows that glycosylation is not required for activity. IL3 sequences are evolutionarily less well conserved with human and murine IL3 sharing approximately 29% homology (at the protein level) and murine and rat IL3 sharing approximately 54% homology. IL3 receptors are expressed on macrophages, mast cells, eosinophils, megakaryocytes, basophils, bone marrow progenitor cells and various myeloid leukemia cells. Binding of IL3 to its receptor causes specific phosphorylation of a 150 kDa membrane glycoprotein. Recombinant human IL3 is a non-glycosylated globular protein.
Gene Symbol IL3
Gene ID 3562
Accession No. P08700
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 15.0 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 ED50 as determined by the dose-dependent proliferation of Human TF-1 cells was found less than 0.5 ng/mL
Bioactivity Data Click To Enlarge
Formulation Lyophilized from a 0.2 μm filtered solution in Phosphate Buffer and NaCl (pH 6.3)
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.