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IL-8 Protein (AA 23-99)

Recombinant IL-8 protein expressed in HEK-293 Cells.
Catalog No. ABIN7317013

Quick Overview for IL-8 Protein (AA 23-99) (ABIN7317013)

Target

See all IL-8 (IL8) Proteins
IL-8 (IL8) (Interleukin 8 (IL8))

Protein Type

Recombinant

Origin

  • 29
  • 5
  • 4
  • 4
  • 4
  • 4
  • 3
  • 3
  • 3
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Human

Source

  • 37
  • 13
  • 10
  • 4
  • 1
  • 1
  • 1
HEK-293 Cells

Purity

> 95 % as determined by reducing SDS-PAGE.
  • Protein Characteristics

    AA 23-99

    Purpose

    Recombinant Human IL-8/CXCL8 Protein (aa 23-99)

    Sequence

    Ala 23-Ser 99

    Characteristics

    The 77 amino acid endothelial-cell derived form (Ala 23-Ser 99) of the mature human IL8 (NP_000575.1) was expressed and purified.

    Endotoxin Level

    < 1.0 EU per μg as determined by the LAL method.
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  • Restrictions

    For Research Use only
  • Format

    Lyophilized

    Reconstitution

    Please refer to the printed manual for detailed information.

    Buffer

    Lyophilized from sterile 100 mM NaCl, 50 mM Tris, pH 7.5

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target

    IL-8 (IL8) (Interleukin 8 (IL8))

    Alternative Name

    IL-8/CXCL8

    Background

    Background: Interleukin 8 (IL-8), also known as CXCL8, which is a chemokine with a defining CXC amino acid motif that was initially characterized for its leukocyte chemotactic activity, is now known to possess tumorigenic and proangiogenic properties as well. This chemokine is secreted by a variety of cell types including monocyte/macrophages, T cells, neutrophils, fibroblasts, endothelial cells, and various tumor cell lines in response to inflammatory stimuli (IL1, TNF, LPS, etc). In human gliomas, IL-8 is expressed and secreted at high levels both in vitro and in vivo, and recent experiments suggest it is critical to glial tumor neovascularity and progression. Levels of IL-8 correlate with histologic grade in glial neoplasms, and the most malignant form, glioblastoma, shows the highest expression in pseudopalisading cells around necrosis, suggesting that hypoxia/anoxia may stimulate expression. Interleukin (IL)-8/CXCL8 is a potent neutrophil chemotactic factor. Accumulating evidence has demonstrated that various types of cells can produce a large amount of IL-8/CXCL8 in response to a wide variety of stimuli, including proinflammatory cytokines, microbes and their products, and environmental changes such as hypoxia, reperfusion, and hyperoxia. Numerous observations have established IL-8/CXCL8 as a key mediator in neutrophil-mediated acute inflammation due to its potent actions on neutrophils. However, several lines of evidence indicate that IL-8/CXCL8 has a wide range of actions on various types of cells, including lymphocytes, monocytes, endothelial cells, and fibroblasts, besides neutrophils. The discovery of these biological functions suggests that IL-8/CXCL8 has crucial roles in various pathological conditions such as chronic inflammation and cancer. IL-8 has been associated with tumor angiogenesis, metastasis, and poor prognosis in breast cancer. IL-8 may present a novel therapeutic target for estrogen driven breast carcinogenesis and tumor progression.

    Synonym: Interleukin-8, 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, GCP1,IL8,Interleukin-8,LECT,LUCT,LYNAP,MDNCF,MONAP,NAF,NAP-1,NAP1

    Molecular Weight

    8 kDa

    NCBI Accession

    NP_000575

    Pathways

    TLR Signaling, Cellular Response to Molecule of Bacterial Origin, Regulation of G-Protein Coupled Receptor Protein Signaling, ER-Nucleus Signaling, Hepatitis C, Autophagy
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