Human Recombinant CXCL8 protein (V2LY-0526-LY4961)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Protein Construction
This product is Human Recombinant CXCL8 protein consist of Amino Acid: 23-99 and predicts a molecular mass of 8 kDa.
Molecule Mass
8 kDa
Sequence
Amino Acid: 23-99
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
C-X-C motif chemokine ligand 8
Function
IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively.
Biological Process
Angiogenesis Source: UniProtKB
Antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
Calcium-mediated signaling Source: UniProtKB
Cell cycle arrest Source: UniProtKB
Cellular response to fibroblast growth factor stimulus Source: UniProtKB
Cellular response to interleukin-1 Source: UniProtKB
Cellular response to lipopolysaccharide Source: BHF-UCL
Cellular response to tumor necrosis factor Source: UniProtKB
Chemokine-mediated signaling pathway Source: GO_Central
Chemotaxis Source: UniProtKB
Cytokine-mediated signaling pathway Source: Reactome
Embryonic digestive tract development Source: DFLAT
G protein-coupled receptor signaling pathway Source: Reactome
Induction of positive chemotaxis Source: UniProtKB
Inflammatory response Source: GO_Central
Intracellular signal transduction Source: UniProtKB
Killing of cells of other organism Source: UniProtKB
Negative regulation of cell adhesion molecule production Source: ARUK-UCL
Negative regulation of cell population proliferation Source: ProtInc
Negative regulation of gene expression Source: ARUK-UCL
Negative regulation of G protein-coupled receptor signaling pathway Source: UniProtKB
Neutrophil activation Source: UniProtKB
Neutrophil chemotaxis Source: UniProtKB
PERK-mediated unfolded protein response Source: Reactome
Positive regulation of angiogenesis Source: CACAO
Positive regulation of cellular biosynthetic process Source: ARUK-UCL
Positive regulation of gene expression Source: ARUK-UCL
Positive regulation of neutrophil chemotaxis Source: BHF-UCL
Receptor internalization Source: UniProtKB
Regulation of cell adhesion Source: UniProtKB
Regulation of entry of bacterium into host cell Source: AgBase
Regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
Response to endoplasmic reticulum stress Source: UniProtKB
Response to molecule of bacterial origin Source: BHF-UCL
Signal transduction Source: ProtInc
Cellular Location
Secreted
PTM
Several N-terminal processed forms are produced by proteolytic cleavage after secretion from at least peripheral blood monocytes, leukcocytes and endothelial cells. In general, IL-8(1-77) is referred to as interleukin-8. IL-8(6-77) is the most promiment form.
Citrullination at Arg-27 prevents proteolysis, and dampens tissue inflammation, it also enhances leukocytosis, possibly through impaired chemokine clearance from the blood circulation.

Nie, G., Cao, X., Mao, Y., Lv, Z., Lv, M., Wang, Y., ... & Liu, C. (2021). Tumor-associated macrophages-mediated CXCL8 infiltration enhances breast cancer metastasis: Suppression by Danirixin. International Immunopharmacology, 95, 107153.

Rasool, M., Pushparaj, P. N., & Karim, S. (2021). Overexpression of CXCL8 gene in Saudi colon cancer patients. Saudi journal of biological sciences, 28(11), 6045-6049.

Li, J., Liu, Q., Huang, X., Cai, Y., Song, L., Xie, Q., ... & Zeng, F. (2020). Transcriptional profiling reveals the regulatory role of CXCL8 in promoting colorectal cancer. Frontiers in Genetics, 10, 1360.

Łukaszewicz-Zając, M., Pączek, S., Mroczko, P., & Kulczyńska-Przybik, A. (2020). The significance of CXCL1 and CXCL8 as well as their specific receptors in colorectal cancer. Cancer Management and Research, 12, 8435.

Hosono, M., Koma, Y. I., Takase, N., Urakawa, N., Higashino, N., Suemune, K., ... & Yokozaki, H. (2017). CXCL8 derived from tumor-associated macrophages and esophageal squamous cell carcinomas contributes to tumor progression by promoting migration and invasion of cancer cells. Oncotarget, 8(62), 106071.

Amrouche, L., Desbuissons, G., Rabant, M., Sauvaget, V., Nguyen, C., Benon, A., ... & Anglicheau, D. (2017). MicroRNA-146a in human and experimental ischemic AKI: CXCL8-dependent mechanism of action. Journal of the American Society of Nephrology, 28(2), 479-493.

Shen, T., Yang, Z., Cheng, X., Xiao, Y., Yu, K., Cai, X., ... & Li, Y. (2017). CXCL8 induces epithelial-mesenchymal transition in colon cancer cells via the PI3K/Akt/NF-κB signaling pathway. Oncology reports, 37(4), 2095-2100.

Shen, L., Zhang, P., Zhang, S., Xie, L., Yao, L., Lang, W., ... & Ji, L. (2017). C‑X‑C motif chemokine ligand 8 promotes endothelial cell homing via the Akt‑signal transducer and activator of transcription pathway to accelerate healing of ischemic and hypoxic skin ulcers. Experimental and Therapeutic Medicine, 13(6), 3021-3031.

Sharkey, D. J., Tremellen, K. P., Briggs, N. E., Dekker, G. A., & Robertson, S. A. (2017). Seminal plasma pro-inflammatory cytokines interferon-γ (IFNG) and CXC motif chemokine ligand 8 (CXCL8) fluctuate over time within men. Human Reproduction, 32(7), 1373-1381.

Yin, Z., Huang, J., Ma, T., Li, D., Wu, Z., Hou, B., & Jian, Z. (2017). Macrophages activating chemokine (CXC motif) ligand 8/miR-17 cluster modulate hepatocellular carcinoma cell growth and metastasis. American journal of translational research, 9(5), 2403.

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For research use only. Not intended for any clinical use.

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