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Recombinant Human IL8 (77aa)

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Product Source Size Cat. No. Price
Recombinant Human IL8 (77aa) E. coli25 µg Z101615 $70.00
100 µg Z101617 $210.00
1.0 mg Z101619 $1,350.00
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Data Sheet
Print Version
Alternative Names IL-8, C-X-C motif chemokine 8, Emoctakin, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil chemotactic factor, MDNCF, Monocyte-derived neutrophil-activating peptide, MONAP, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, T cell chemotactic factor
Recombinant Human Interleukin-8 (77AA) (IL8)
Description IL8 is produced by stimulated monocytes but not by tissue macrophages and T-lymphocytes. In many cell types the synthesis of IL8 is strongly stimulated by IL1, TNF-alpha and bacterial lipopolysaccharides. The expression of IL8 from resting and stimulated human blood monocytes is up-regulated by IL7. The IL8 receptor (CD128) is a dimeric glycoprotein consisting of a 59 kDa and a 67 kDa subunit. It is expressed in many different cell types including those not responding to IL8. IL8 differs from all other cytokines in its ability to specifically activate neutrophil granulocytes. IL8 also enhances the metabolism of reactive oxygen species and increases chemotaxis and the enhanced expression of adhesion molecules. Recombinant Human IL8 (77aa) represents the construct spanning residues 23 to 99, inclusive.
Gene Symbol IL8
Gene ID 3576
Accession No. P10145
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 9.0 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 dose dependent proliferation of endothelial cells was found to be <0.5ng/ml
Formulation Lyophilized from a 0.2 μm filtered solution in Phosphate buffer and NaCl (pH 7.5)
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
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.