IL 8 Porcine

Interleukin-8 (1-72 a.a) Porcine Recombinant (CXCL8)

This recombinant porcine Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 78 amino acids. With a molecular weight of 9.1kDa, it is purified using proprietary chromatographic techniques to ensure high quality.
Shipped with Ice Packs
Cat. No.
BT15346
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder, sterile-filtered for purity.

IL 8 Rhesus Macaque

Interleukin-8 Rhesus Macaque Recombinant

IL-8 Rhesus Macaque Recombinant is a non-glycosylated protein produced in E. coli. It consists of a single polypeptide chain with 79 amino acids and has a molecular weight of 9.1kDa. This purified protein is obtained through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15442
Source
Escherichia Coli.
Appearance
The product appears as a white, sterile, and lyophilized (freeze-dried) powder.

IL 8 Canine

Interleukin-8 Canine Recombinant

Recombinant Canine Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain with 79 amino acids and a molecular weight of 9.1kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14911
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder

IL 8 Human (1-72)

Interleukin-8 (1-72 a.a.) Human Recombinant (CXCL8)

Recombinant Human Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 72 amino acids. With a molecular mass of 8452 Daltons, this purified protein is obtained through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14990
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized powder

IL 8 Human (1-77), His

Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8), His Tag

Recombinant Human Interleukin-8, produced in E. coli, is a non-glycosylated polypeptide chain comprising 77 amino acids (fragment 23-99). With a molecular weight of 13.7 kDa, it features an amino-terminal hexahistidine tag. Purification of IL-8 His is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT15177
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

IL 8 Human, Pichia

Interleukin-8 (1-77 a.a.) Human Recombinant, (CXCL8) Pichia

This product consists of a single chain of 79 amino acids, representing the recombinant form of human Interleukin-8, produced in yeast (Pichia pastoris). The protein has undergone glycosylation, a common post-translational modification, and exhibits a molecular weight of 9 kDa. Purification is achieved using specialized chromatographic methods, ensuring high purity.
Shipped with Ice Packs
Cat. No.
BT15265
Source
Pichia Pastoris.
Appearance
This product, in its lyophilized form, presents as a white powder, free from any particulate matter and sterilized through filtration.

IL 8 Human (1-77)

Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)

Recombinant Human Interleukin-8, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 77 amino acids. With a molecular weight of 8904 Daltons, this purified protein is obtained through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15090
Source
Escherichia Coli.
Appearance
White, sterile-filtered, lyophilized powder.

IL8 Canine, HEK

Interleukin-8, HEK Canine Recombinant

IL8 Canine, HEK Recombinant, produced in HEK293 cells, is a single, glycosylated polypeptide chain containing 80 amino acids (28-101 a.a) with a molecular mass of 9.4 kDa. It features a 6 amino acid His tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT15516
Source

HEK293 Cells.

Appearance
Sterile filtered colorless solution.

IL8 GST

Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag

Recombinant Human Interleukin-8, comprising 72 amino acids, is produced in E. coli. This protein is fused to a GST tag at its N-terminus and purified using a proprietary chromatographic technique.
Shipped with Ice Packs
Cat. No.
BT15598
Source

Escherichia Coli.

Appearance
Sterile Filtered clear solution.
Definition and Classification

Interleukin 8 (CXCL8), also known as chemokine (C-X-C motif) ligand 8, is a member of the CXC chemokine family. It is a small cytokine produced by various cell types, including macrophages, epithelial cells, and endothelial cells . CXCL8 is primarily known for its role in chemotaxis, attracting neutrophils to sites of infection or inflammation .

Biological Properties

Key Biological Properties: CXCL8 is a potent neutrophil chemoattractant and activator. It induces chemotaxis in target cells, primarily neutrophils, causing them to migrate toward the site of infection .

Expression Patterns: CXCL8 is expressed by a variety of cells, including monocytes, macrophages, neutrophils, T lymphocytes, epithelial cells, and fibroblasts . Its expression is upregulated in response to inflammatory stimuli.

Tissue Distribution: CXCL8 is found in various tissues, including periodontal fiber, granulocytes, beta cells, cartilage tissue, olfactory zone of nasal mucosa, monocytes, mucosa of paranasal sinus, bone marrow cells, sperm, and gallbladder .

Biological Functions

Primary Biological Functions: CXCL8 plays a crucial role in the immune response by attracting neutrophils to sites of infection or injury . It also stimulates phagocytosis and promotes angiogenesis .

Role in Immune Responses: CXCL8 is involved in the recruitment and activation of neutrophils, which are essential for the innate immune response . It also plays a role in pathogen recognition and clearance.

Modes of Action

Mechanisms with Other Molecules and Cells: CXCL8 interacts with its receptors, CXCR1 and CXCR2, on the surface of target cells . This interaction triggers a series of downstream signaling cascades that lead to various cellular responses, including chemotaxis, degranulation, and respiratory burst .

Binding Partners: CXCL8 binds to glycosaminoglycans and its receptors, CXCR1 and CXCR2 . These interactions are crucial for its biological activity.

Downstream Signaling Cascades: Upon binding to its receptors, CXCL8 activates several signaling pathways, including the G protein-coupled receptor signaling pathway, intracellular signal transduction, and chemokine-mediated signaling pathway .

Regulatory Mechanisms

Transcriptional Regulation: The expression of CXCL8 is regulated by various transcription factors, including NF-κB and AP-1 . These factors bind to the CXCL8 promoter and enhance its transcription in response to inflammatory stimuli.

Post-Translational Modifications: CXCL8 undergoes post-translational modifications, including cleavage to generate active isoforms . These modifications are essential for its biological activity.

Other Regulatory Mechanisms: The expression of CXCL8 is also regulated by miRNAs, such as miRNA-146a/b-5p, which indirectly repress its expression by silencing the expression of IRAK1 .

Applications

Biomedical Research: CXCL8 is widely studied in the context of inflammation, cancer, and autoimmune diseases . It serves as a biomarker for various inflammatory conditions and is a target for therapeutic interventions.

Diagnostic Tools: Elevated levels of CXCL8 are associated with various diseases, including cancer and inflammatory disorders . It is used as a diagnostic marker to assess disease severity and progression.

Therapeutic Strategies: Targeting the CXCL8-CXCR1/2 axis is a promising therapeutic approach for treating inflammatory diseases and cancer . Inhibitors of CXCL8 and its receptors are being developed and tested in clinical trials.

Role in the Life Cycle

Development: CXCL8 plays a role in embryonic development by regulating the migration and activation of hematopoietic progenitor cells .

Aging: The expression of CXCL8 increases with age, contributing to age-related inflammation and immune dysregulation .

Disease: CXCL8 is implicated in various diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions . It promotes tumor growth, metastasis, and angiogenesis in the tumor microenvironment .

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