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Recombinant Human IL7


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Product Source Size Cat. No. Price
Recombinant Human IL7 CHO cells 25 µg Z101325 $760.00
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Data Sheet
Print Version
Alternative Names Il-7
Recombinant Human Interleukin-7 (IL7)
Description IL-7 is secreted constitutively into the conditioned medium of adherent bone marrow stromal cells and thymic cells. Mouse and human keratinocytes have been shown also to express and secrete IL7. Human IL-7 (152 amino acids; 17.4 kDa) and murine IL-7 (129 amino acids) show 60% sequence homology at the protein level. The human IL-7 receptor is an integral strongly glycosylated membrane proteins of 76 kDa expressed on activated T cells. This receptor has been designated as CD127. IL-7 receptors are expressed on pre-B cells and their progenitors. They are not expressed on mature B cells. IL-7 receptors are expressed also on bone marrow macrophages. Functional IL-7 receptors are found on the cell surface of multiphenotypic, biphenotypic, and immature lymphoid progenitors of B cells with the gene arrangement of the heavy immunoglobulin chain such as those observed in the germ line.
Gene Symbol IL7
Gene ID 3574
Accession No. P13232
Source CHO cells
Appearance Lyophilized Powder
Molecular Weight 17.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Bioactivity The ED(50) determined by dose-dependent stimulation of the proliferation of murine 2E8 cells is ≤ 0.5 ng/mL, corresponding to a specific activity of ≥ 2.0 x 10^6 units/mg.
Formulation Recombinant Interleukin-7 was lyophilized from a 0.2 μm filtered PBS solution pH 4.5.
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.