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Human Recombinant IL8 (prokaryotic) (from E.coli)
  MSPP-RPA080HU1
 :  
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Human Recombinant IL8 (prokaryotic) (from E.coli)
  MSPP-RPA080HU1
 :  RPA080HU01
 :  

 

  • Pack type:
    Vial
  • Conjugation:
    Unconjugated
  • Protein Function:
    Cytokine
  • Protein/Peptide Type:
    Recombinant
  • Source:
    E. coli
  • Species:
    Human
  • Size:
    50 µg
  • Tag sequence:
    MGHHHHHHSGSEF
  • Storage Conditions:
    −20 °C
  • Endotoxin Content:
    <1.0 EU per 1 µg (determined by the LAL method)
  • Gene ID:
    3576
  • Reconstitution Instructions:
    Reconstitute in 10 mM PBS (pH 7.4) to a concentration of 0.1 - 1.0 mg/ml. Do not vortex.
  • Endotoxin-free:
    N
  • Carrier-Free:
    Y
  • Protease-free:
    N
  • Animal-Free:
    Y
  • Protein Synonyms:
    Interleukin 8
  • UniProtKB:
    p10145
  • Protein/Peptide Name:
    IL8 (prokaryotic)
  • Purity:
    97 - 100%
  • Molecular Weight:
    12 kDa
  • Sequence:
    Ser28~Ser99
  • Endotoxin Level:
    Low
  • Concentration:
    0.2 mg/ml
  • Formulation:
    Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose
  • Nuclease-free:
    N
  • Shipping Temperature:
    4 °C
  • Tested Applications:
    Positive control, Immunogen, SDS-PAGE, Western blot.
  • Cat. No.:
    MSPP-RPA080HU1

 

 

This is a IL8 recombinant protein (prokaryotic), Human is sequencing from Ser28~Ser99 with 97 to 100% purity. Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose with 0.2 mg/ml.

  • High quality, purity, reproducibility and effectiveness
  • Offers customized buffers and tag options
  • 100% quality and service satisfaction guarantee

Interleukin 8 (IL-8), a member of the neutrophil-specific CXC subfamily of chemokines, is a potent neutrophil chemotactic and activating factor. It is a primary inflammatory cytokine produced by many cells in response to proinflammatory stimuli such as IL-1, TNF, LPS and viruses. Its function is, in part, to attract neutrophils to the site of inflammation and to activate them. The IL-8 cDNA sequence predicts a protein of 99 amino acids. Removal of a 22-residue signal peptide generates a mature protein of 77 amino acids (~8 kDa). Further proteolysis of the N-terminal end leads to a variant form with 72 amino acids; full activation of IL-8 may require cleavage to the 72 amino acid form. IL-8 can form non-covalent dimers in solution, especially at high concentrations, but dimerization is not necessary for biological activity.

 : ISO 9001 and ISO 13485 certified, three level QC system.
 : For research use only. Not for use in clinical diagnostic procedures. Please proper stored each component based on the instruction.