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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].
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].
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 (CHO) is produced in CHO cells, and consists of 77 amino acids (A23-S99).
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).
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 (HEK293, His) is produced in HEK293 cells with six C-Terminal His-tags. It consists of 79 amino acids (E21-S99).
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 (72a.a) is produced in E.coil, and consists of 72 amino acids (S28-S99).
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, HEK293) is produced in HEK293 cells, and consists of 77 amino acids (A23-S99).
IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. Animal-Free IL-8/CXCL8 Protein, Human (His) is the recombinant human-derived animal-FreeIL-8/CXCL8 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free IL-8/CXCL8 Protein, Human (His) is 72 a.a., with molecular weight of ~9.32 kDa.
CXCL8 protein, a crucial chemotactic factor, drives inflammatory responses by attracting neutrophils, basophils, and T-cells, contributing to pathogen clearance. It plays a pivotal role in activating neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. CXCL8 homodimerizes and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. CXCL8 Protein, Rhesus macaque (His) is the recombinant Rhesus Macaque-derived CXCL8 protein, expressed by E. coli , with N-6*His labeled tag. The total length of CXCL8 Protein, Rhesus macaque (His) is 79 a.a., with molecular weight of ~11 kDa.
IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. IL-8/CXCL8 Protein, Porcine is the recombinant Porcine-derived IL-8/CXCL8 protein, expressed by E. coli , with tag free. The total length of IL-8/CXCL8 Protein, Porcine is 79 a.a., with molecular weight of ~12.97 kDa.
IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. IL-8/CXCL8 Protein, Human is the recombinant human-derived IL-8/CXCL8 protein, expressed by E. coli , with tag free. The total length of IL-8/CXCL8 Protein, Human is 77 a.a., with molecular weight of ~11.0 kDa.
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 (72a.a, HEK293, Fc) is produced in HEK293 cells with a N-Terminal Fc-tag. It consists of 72 amino acids (S28-S99).
Interleukin-8; IL-8; GCP-1; MDNCF; MONAP; NAP-1; GCP/IL-8 protein IV; IL8/NAP1 form I; CXCL8; LECT; LUCT; LYNAP; NAF
Cynomolgus
HEK293
IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. IL-8/CXCL8 Protein, Cynomolgus (HEK293, C-His) is the recombinant cynomolgus-derived IL-8/CXCL8 protein, expressed by HEK293 , with C-His labeled tag. The total length of IL-8/CXCL8 Protein, Cynomolgus (HEK293, C-His) is 78 a.a., with molecular weight of 12-14 kDa.
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, Canine is produced in E.coil, and consists of 79 amino acids (A23-P101).
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, Rhesus Macaque is produced in E.coil, and consists of 79 amino acids (A23-P101).
IL-8/CXCL8 protein, a vital chemotactic factor, orchestrates inflammatory responses by attracting neutrophils, basophils, and T-cells to clear pathogens. It activates neutrophils and binds to CXCR1/CXCR2 receptors, initiating downstream signaling pathways. IL-8/CXCL8 homodimerizes, disrupted by tick evasin-3, and interacts with TNFAIP6, potentially regulating chemokine activity in the inflammatory microenvironment. Animal-Free IL-8/CXCL8 Protein, Pig (His) is the recombinant pig-derived animal-FreeIL-8/CXCL8 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free IL-8/CXCL8 Protein, Pig (His) is 78 a.a., with molecular weight of ~10.04 kDa.
