Datasheet

Biological Description

Specificity	Anti-CX3CL1/Fractalkine Chemokine Domain Rat Antibody [K3M15] detects endogenous levels of total CX3CL1/Fractalkine Chemokine Domain protein.
Background	CX3CL1, also known as fractalkine, is the only member of the CX3C chemokine family and is distinguished by three amino acids separating its first two conserved cysteine residues. It is synthesized as a 373-amino acid type I transmembrane protein consisting of four major domains: an N-terminal chemokine domain that mediates chemoattraction, a mucin-like stalk that supports cell adhesion, a transmembrane segment that anchors the protein to the cell surface, and a cytoplasmic domain involved in intracellular signaling. Fractalkine uniquely exhibits both chemotactic and adhesive properties, acting as a membrane-bound adhesion molecule and, upon cleavage by metalloproteinases ADAM10 and ADAM17, functioning as a soluble chemoattractant. Its receptor, CX3CR1, is a G protein-coupled receptor expressed on immune and vascular cells, including monocytes, macrophages, NK cells, T cells, and smooth muscle cells. The binding of CX3CL1 to CX3CR1 activates multiple signaling pathways, including PI3K, MAPK, AKT, Src, and eNOS, which regulate immune cell adhesion, migration, survival, and resistance to apoptosis. The CX3CL1–CX3CR1 axis is involved in key physiological processes such as immune surveillance, angiogenesis, and tissue repair, while also contributing to the pathogenesis of conditions like atherosclerosis, cancer, and neuroinflammation by promoting inflammatory cell recruitment and vascular dysfunction. Genetic variants in CX3CR1 can alter receptor activity and influence individual susceptibility to inflammatory and degenerative diseases.

Specificity

Anti-CX3CL1/Fractalkine Chemokine Domain Rat Antibody [K3M15] detects endogenous levels of total CX3CL1/Fractalkine Chemokine Domain protein.

Background

CX3CL1, also known as fractalkine, is the only member of the CX3C chemokine family and is distinguished by three amino acids separating its first two conserved cysteine residues. It is synthesized as a 373-amino acid type I transmembrane protein consisting of four major domains: an N-terminal chemokine domain that mediates chemoattraction, a mucin-like stalk that supports cell adhesion, a transmembrane segment that anchors the protein to the cell surface, and a cytoplasmic domain involved in intracellular signaling. Fractalkine uniquely exhibits both chemotactic and adhesive properties, acting as a membrane-bound adhesion molecule and, upon cleavage by metalloproteinases ADAM10 and ADAM17, functioning as a soluble chemoattractant. Its receptor, CX3CR1, is a G protein-coupled receptor expressed on immune and vascular cells, including monocytes, macrophages, NK cells, T cells, and smooth muscle cells. The binding of CX3CL1 to CX3CR1 activates multiple signaling pathways, including PI3K, MAPK, AKT, Src, and eNOS, which regulate immune cell adhesion, migration, survival, and resistance to apoptosis. The CX3CL1–CX3CR1 axis is involved in key physiological processes such as immune surveillance, angiogenesis, and tissue repair, while also contributing to the pathogenesis of conditions like atherosclerosis, cancer, and neuroinflammation by promoting inflammatory cell recruitment and vascular dysfunction. Genetic variants in CX3CR1 can alter receptor activity and influence individual susceptibility to inflammatory and degenerative diseases.

Usage Information

Application

WB, ELISA

Dilution

WB

1:2000

Reactivity

Mouse

Source

Rat

MW

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/33391453/
https://pubmed.ncbi.nlm.nih.gov/24556958/

Anti-CX3CL1/Fractalkine Chemokine Domain Rat Antibody [K3M15]

Biological Description

Usage Information

References

Application Data