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  5. IL-8/CXCL8
  6. IL-8/CXCL8 Protein, Human (77a.a)

IL-8/CXCL8 Protein, Human (77a.a)

Cat. No.: HY-P7224
COA Handling Instructions

Interleukin-8 (IL-8), also known as CXCL8 or NAP-1, is a pro-inflammatory CXC chemokine. IL-8 acts on human neutrophils via two receptors, CXCR1 and CXCR2. IL-8 has a conserved Glu-Leu-Arg (ELR) N-terminal motif, and is an agonist for CXCR1/CXCR2. IL-8 is produced by various cells including leukocytes, endothelial cells, and epithelial cells. IL-8/CXCL8 Protein, Human (77a.a) is produced in E.coil, and consists of 77 amino acids (A23-S99).

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Description

Interleukin-8 (IL-8), also known as CXCL8 or NAP-1, is a pro-inflammatory CXC chemokine. IL-8 acts on human neutrophils via two receptors, CXCR1 and CXCR2. IL-8 has a conserved Glu-Leu-Arg (ELR) N-terminal motif, and is an agonist for CXCR1/CXCR2. IL-8 is produced by various cells including leukocytes, endothelial cells, and epithelial cells[1][2][3]. IL-8/CXCL8 Protein, Human (77a.a) is produced in E.coil, and consists of 77 amino acids (A23-S99).

Background

IL-8 (CXCL8) belongs to the ELR+ CXC chemokines family. IL-8 is initially produced as a protein of 99 amino acids that undergoes cleavage to form active IL-8 isoforms, a 77 amino acid peptide in non-immune cells or a 72 amino acid peptide in monocytes and macrophages. The gene encoding IL-8 is located on chromosome 4q13-q21. Dimerisation of IL-8 forms the structural basis for receptor binding. IL-8 is expressed by various cells including monocytes, macrophages, leukocytes, endothelial cells, and epithelial cells[1][2][3].
Mature human IL-8/CXCL8 shares 75% amino acid sequence identity with canine IL-8/CXCL8. While, human IL-8 shares 94.95% aa sequence identity with Rhesus Macaque IL-8 protein.
IL-8 is responsible for the recruitment and activation of neutrophils and granulocytes to the site of inflammation. IL-8 is almost undetectable in physiological states, but is rapidly induced by pro-inflammatory cytokines such as TNFα and IL-1β. The function of IL-8 mainly relies on its interaction with specific cell surface GPCR, CXCR1 and CXCR2. In addition, IL-8 is reported to promote integrin β3 upregulation and the invasion of hepatocellular carcinoma cells through activation of the PI3K/Akt pathway. In odontogenic lesions, IL-8 has been proven to be highly expressed in ameloblastoma epithelial cells and irreversible pulpitis. In rheumatoid arthritis and other inflammatory joint diseases IL-8 could bring about the accumulation of neutrophils, which are considered a major source of cartilage-degrading enzymes. IL-8 stimulates the MAPK and tyrosine phosphorylation of cellular proteins. Tumour cells and fibroblasts communicate with each other, including autocrine and paracrine factors, including IL-8, resulting in the upregulation of MMP2 and MMP9 degradable extracellular matrix (ECM) components that trigger tumour invasion[1][2][3][4].
  IL-8 is typically known to promote angiogenesis, but it also activates matrix metalloproteinase (MMP) that is involved in metastasisrelated tissue remodelling. IL-8 is induced in lipopolysaccharide (LPS)-stimulated monocytes and shown to induce neutrophil migration. IL-8 exerts multiple effects on biological activities of tumour cells including proliferation, invasion and migration. IL-8 also increases the expression of Akt in androgen-independent prostate cancer (AIPC) cell lines. IL-8 activates MAPK signalling via PI3K in neutrophils, and via transactivation of EGFR resulting in Ras-GTPase activation in ovarian and lung cancer cell lines. There is substantial amount of experimental data suggesting that IL-8 and receptors contribute to elimination of pathogens, but may also contribute significantly to disease-associated processes, including tissue injury, fibrosis, angiogenesis and tumorigenesis[3][5].

In Vitro

Recombinant human IL-8 (10, 30, and 100 μg/kg; single intravenous injection) injected into rhesus monkeys (2-3 years; 2.5-4.5 kg). IL-8 injection results in instant neutropenia that was due to pulmonary sequestration. Within 30 minutes after IL-8 injection, neutrophilia developed with counts up to 10-fold greater than baseline levels. The numbers of hematopoietic progenitor cells (HPCs) increased of blood at 30 minutes after injection of 100 μg/kg IL-8[7].

In Vivo

Recombinant human IL-8/CXCL8 (100 ng/mL; for 24-96 h) stimulation leads to enhancement of invasion and suppression of late stage apoptosis in MG-63 cells. Moreover, secretions of MMPs by MG-63 cells are also increased upon stimulation. CXCL8 induces the elevations of phosphorylated PI3K and Akt, but not PKC or FAK[6].

Biological Activity

1.The ED50 is <150 ng/mL as measured by CHO-K1/Gα15/hCXCR1 cells (human Gα15 and human CXCR1 stably expressed in CHO-K1 cells).
2.Immobilized Human IL-8 at 2 μg/mL (100 μL/well) can bind Anti-IL-8 Antibody. The ED50 for this effect is 28.35 ng/mL.

  • Immobilized Human IL-8 at 2 μg/mL (100 μL/well) can bind Anti-IL-8 Antibody, The ED50 for this effect is 28.35 ng/mL.
Species

Human

Source

E. coli

Tag

Tag Free

Accession

P10145 (A23-S99)

Gene ID
Synonyms
rHuIL-8/CXCL8; C-X-C motif chemokine 8; Emoctakin; MDNCF; NAP-1; IL8
AA Sequence

AVLPRSAKELRCQCIKTYSKPFHPKFIKELRVIESGPHCANTEIIVKLSDGRELCLDPKENWVQRVVEKFLKRAENS

Molecular Weight

Approximately 8.9 kDa

Purity

Greater than 95% as determined by reducing SDS-PAGE.

Appearance

Lyophilized powder

Formulation

Lyophilized after extensive dialysis against PBS or sterile 50 mM Tris-HCL, 300 mM NaCL, pH 8.0.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Storage & Stability

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Shipping

Room temperature in continental US; may vary elsewhere.

Documentation
References

IL-8/CXCL8 Protein, Human (77a.a) Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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IL-8/CXCL8 Protein, Human (77a.a)
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HY-P7224
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