Recombinant Human CX3CL1/Fractalkine (Chemokine Domain) protein
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human CX3CL1/Fractalkine (Chemokine Domain) protein is a Human Fragment protein, in the 25 to 339 aa range, expressed in HEK 293 cells, with >95%, suitable for SDS-PAGE.
View Alternative Names
FKN, NTT, SCYD1, A-152E5.2, CX3CL1, Fractalkine, C-X3-C motif chemokine 1, CX3C membrane-anchored chemokine, Neurotactin, Small-inducible cytokine D1
- SDS-PAGE
Lab
SDS-PAGE - Recombinant Human CX3CL1/Fractalkine (Chemokine Domain) protein (AB283874)
SDS-page analysis of ab283874.
ab283874 is heavily glycosylated during expression which presents as an unresolved band on the gel.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
CX3CL1 is involved in the immune system and nervous system functions influencing leukocyte adhesion and migration. It is not known to be part of a large multiprotein complex but directly interacts with its fractalkine receptor CX3CR1 on the surface of immune cells. This interaction regulates communication between neurons and microglia which highlights its role in neuroinflammation. CX3CL1's expression and function suggest a significant influence over inflammatory responses and homeostatic balance within these systems.
Pathways
CX3CL1 plays a role in the MAPK and PI3K-Akt pathways vital for cell survival proliferation and migration. Within these pathways CX3CL1 influences and interacts with several proteins thereby modulating inflammatory responses and cellular migration. These pathways are essential for immune system regulation where CX3CL1 acts as a mediator in signal transduction processes that connect immune responses to cellular activities such as proliferation and survival.
Specifications
Form
Lyophilized
General info
Function
Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV : ITGB3 and ITGA4 : ITGB1 (PubMed : 12055230, PubMed : 21829356, PubMed : 23125415, PubMed : 9782118, PubMed : 9931005). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed : 12055230, PubMed : 9024663, PubMed : 9177350, PubMed : 9782118). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed : 9024663, PubMed : 9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (PubMed : 23125415, PubMed : 24789099). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (PubMed : 23125415, PubMed : 24789099). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (PubMed : 23125415, PubMed : 24789099).. Processed fractalkine. The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils.. Fractalkine. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells.. (Microbial infection) Mediates the cytoadherence of erythrocytes infected with parasite P.falciparum (strain 3D7) with endothelial cells by interacting with P.falciparum CBP1 and CBP2 expressed at the surface of erythrocytes (PubMed : 27653778). The adhesion prevents the elimination of infected erythrocytes by the spleen (Probable).
Sequence similarities
Belongs to the intercrine delta family.
Post-translational modifications
A soluble short 95 kDa form may be released by proteolytic cleavage from the long membrane-anchored form.. O-glycosylated with core 1 or possibly core 8 glycans.
Target data
Complementary Products
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com