抗IL-8抗体(Anti-IL-8, Goat-Poly, Biotin antibody)

• 2025/12/01

  試薬 特別価格

  [RSD]厳選 抗体＆リコンビナントタンパク質 30％OFFキャンペーン[～2026/02/27] NEW

  期間：2025/12/01 ～2026/02/27

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  R&D Systems, Inc.（RSD）

• 価格
• Product Details
• Applications and Data
• Related Product & Information

価格

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Product Details

Species Reactivity	Canine
Label	Biotin
Immunogen	E. coli-derived recombinant canine IL-8/CXCL8Ala23-Pro101Accession # P41324
Source	Polyclonal Goat IgG
Purification	Antigen Affinity-purified
Specificity	Detects canine IL-8/CXCL8 in Western blots. In Western blots, less than 1% cross-reactivity with recombinant human IL-8/CXCL8 and recombinant porcine IL-8/CXCL8 is observed.

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Applications and Data

	Recommended Concentration	Sample
Western Blot	0.1 µg/mL	Recombinant Canine IL-8/CXCL8 (Catalog # 1608-CL)
Immunocytochemistry	5-15 µg/mL	Immersion fixed canine lymphocytes

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Related Product & Information

Background

IL-8/CXCL8

background_content

Background: IL-8/CXCL8 Interleukin 8 (IL-8), also named monocyte-derived neutrophil chemotactic factor (MDNCF), neutrophil-activating protein 1 (NAP-1), neutrophil-activating factor (NAF) and granulocyte chemotactic peptide (GCP), belongs to the Glu-Leu-Arg motif containing (ELR+) CXC chemokine family and has been designated CXCL8. IL-8 is a potent neutrophil chemoattractant that recruits neutrophils to sites of inflammation. IL-8 also activates neutrophil functions and through a poorly understood mechanism, promotes angiogenesis. The biological activites of IL-8 is mediated by two types of G protein-coupled chemokine receptors, CXCR1 and CXCR2. In normal tissues, IL-8 expression and secretion is barely detectable. Upon stimulation by a wide range of pro-inflammatory signals including exposure to IL-1, TNF, bacterial or viral products, IL-8 production is rapidly induced in many different cell types. Secreted IL-8 is not glycosylated but has N-terminal sequence heterogenecity due to proteolytic processing. In human, two major forms, the 72 amino acid (aa) monocyte-derived IL-8 and the 77 aa endothelial IL-8 have been identified. Whereas the 72 aa isoform is a more potent chemoattractant, only the 77 aa isoform can induce apoptosis in leukemic cells. The N-terminal pentapeptide in the 77 aa isoform has been identified as the active site for the IL-8 apoptotic activity. Canine IL-8 encodes a 101 aa precursor protein with a putative 22 aa signal peptide. It shares 77% and 87% aa sequence identity with human and porcine IL-8, respectively. Similar to human IL-8, recombinant canine IL-8 also undergoes N‑terminal processing. Two major peptides (the 79 aa and 74 aa variants that differ by an analogous N-terminal pentapeptide) are present in the recombinant canine IL‑8 preparations.

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