Recombinant Mouse Fractalkine / CX3CL1 Protein (His Tag)

Name: Recombinant Mouse Fractalkine / CX3CL1 Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-2137
Availability: InStock

Collections: Chemokines and receptors, Cytokines and growth factors, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	His
Host Species	Mouse
Accession	O35188
Synonym	AB030188, ABCD-3, AI848747, CX3C, Cxc3, D8Bwg0439e, Scyd1
Background	Fractalkine or Chemokine (C-X3-C motif) ligand 1 (CX3CL1) is a member of the CX3C chemokine family. Fractalkine / CX3CL1 is a unique chemokine that functions not only as a chemoattractant but also as an adhesion molecule and is expressed on endothelial cells activated by proinflammatory cytokines, such as interferon-gamma and tumor necrosis factor-alpha. Fractalkine/CX3CL1 is expressed in a membrane-bound form on activated endothelial cells and mediates attachment and firm adhesion of T cells, monocytes and NK cells. Fractalkine / CX3CL1 is associated with dendritic cells (DC) in epidermis and lymphoid organs. The fractalkine receptor, CX3CR1, is expressed on cytotoxic effector lymphocytes, including natural killer (NK) cells and cytotoxic T lymphocytes, which contain high levels of intracellular perforin and granzyme B, and on macrophages. Soluble fractalkine causes migration of NK cells, cytotoxic T lymphocytes, and macrophages, whereas the membrane-bound form captures and enhances the subsequent migration of these cells in response to secondary stimulation with other chemokines.
Description	A DNA sequence encoding the mouse Cx3cl1 (O35188) (Gln25-Lys105) was expressed with a His tag at the C-terminus.
Source	Yeast
Predicted N Terminal	Gln 25
AA Sequence	Gln25-Lys105
Molecular Weight	The recombinant mouse Cx3cl1 consists of 91 a.a. and predicts a molecular mass of 10.7 kDa.
Purity	>95% as determined by SDS-PAGE.
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS,PH7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein 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.

Target Details

Target Function	Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the endothelium. Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner. In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins. 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.; The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils.; The membrane-bound form promotes adhesion of those leukocytes to endothelial cells.
Subcellular Location	Cell membrane; Single-pass type I membrane protein.; [Processed fractalkine]: Secreted.
Protein Families	Intercrine delta family
Database References	KEGG: mmu:20312 STRING: 10090.ENSMUSP00000034230 UniGene: Mm.103711
Tissue Specificity	Highest levels in brain. Lower levels in kidney, heart and lung. Also found in skeletal muscle and testis. Highly expressed in lesional smooth muscle cells, but not macrophages.

Gene Functions References

The data of this study suggested that overexpression of only chemokine domain of CX3CL1 does not protect against tau pathology. PMID: 30253780
the CX3CL1/CX3CR1 axis contributes to the proliferative and pro-inflammatory effects of Ang II in VSMCs. PMID: 29356931
that CX3CL1-CX3CR1 signaling is a molecular mechanism capable of modulating microglial-mediated degeneration PMID: 27314452
CXCR4(+) CD45(-) bone marrow cells are niche forming for osteoclastogenesis via the SDF-1, CXCL7, and CX3CL1 signaling pathways in bone marrow. PMID: 27339271
Increased fractalkine and its receptor CX3CR1 may cause a cross-talk between activated glial cells and neurons, playing an important role in the development of neuroinflammation in fructose-fed mice. PMID: 26765996
miR-223 controls the expression of CX3CL1 by targeting HDAC2 in chronic obstructive pulmonary disease patients and mouse models of the disease. PMID: 26864305
in this study, CX3CL1 is identified as a novel substrate of MMP-19 PMID: 26555704
The CX3CL1/CX3CR1 system is essential for restricting coxsackievirus B3-induced myocarditis. PMID: 28800592
changes in GSK-3beta activity and/or levels regulate the production and subsequent secretion of fractalkine, a chemokine involved in the immune response that has been linked to AD and to other different neurological disorders. PMID: 27832289
Medial ganglionic eminence (MGE) interneurons secrete fractalkine that promotes genesis of oligodendrocytes from glially biased cortical precursors in culture. Moreover, when MGE interneurons are genetically ablated in vivo prior to their migration, this causes a deficit in cortical oligodendrogenesis. PMID: 28472653
our findings reveal a previously unknown regulatory role for LRRK2 in CX3CR1 signalling and suggest that an increase of CX3CR1 activity contributes to the attenuated inflammatory responses in Lrrk2-null microglia PMID: 27378696
a crucial role of CX3CL1-CX3CR1 in experimental colitis, in particular for intestinal leukocyte recruitment during murine colitis, is reported. PMID: 27942903
These results strongly suggest the involvement of CX3CL1 in the migration of osteoclast precursors and osteoclastogenesis. PMID: 27579490
Authors provide evidence that interactions between CX3CL1 and CX3CR1 play crucial roles in determining the number of M1 macrophages within the skin of mice, which in turn can have dramatic effects on psoriasis-like inflammation. PMID: 26976687
In the absence of the rd8 allele, deficiency of CCR2 and CX3CL1 in mice leads to a mild form of retinal degeneration which is associated with the recruitment of macrophages, particularly to the subretinal space. This model enables to assess consequences of perturbed chemokine signaling, but it does not recapitulate cardinal age-related macular degeneration features. PMID: 26670885
Also icariin reduced CX3CR1 and CX3CL1 protein levels in the artery wall. In conclusion, icariin could be a potential anti-atherosclerosis agent by downregulating the expression of CX3CR1. PMID: 26802470
The biological activity of CX3CL1 is regulated by conversion of a membrane integrated to a soluble form during neurogenesis and in response to pathologic changes in the adult retinal milieu. PMID: 25191897
CX3CL1/CX3CR1 signaling is involved in LTP of C-fiber-evoked field potentials in the rodent spinal dorsal horn PMID: 25768734
CX3CL1/CX3CR1-mediated microglial activation plays a detrimental role in ischemic brain via p38MAPK/PKC signaling PMID: 25966946
Cx3cl1 overexpression suppresses alpha-synuclein-mediated neurodegeneration. PMID: 25195598
IFN-gamma induces aberrant CD49b+ NK cell recruitment and pregnancy failure through regulating CX3CL1. PMID: 25375377
Insulin resistance increases plaque vulnerability by augmenting the CX3CL1/CX3CR1 axis, which is mechanistically linked to reduced vascular smooth muscle cell survival PMID: 24788416
Together, these studies challenge the "frustrated phagocytosis" concept and suggest that neuronal-microglial communication link the two central AD pathologies. PMID: 25209291
CX3CL1 may contribute to the regulation of toxigenic C. difficile infection. PMID: 24362517
These results demonstrate that the de novo CX3CL1-CX3CR1 axis plays a pivotal role in osteoclast recruitment and subsequent bone resorption PMID: 24401612
our data suggest that the CX3CR1/ CX3CL1 pathway is involved in the recruitment of circulating CD16 thorn CX3CR1 thorn monocytes to the periprosthetic tissues. PMID: 24700421
Data indicate that atopic dermatitis (AD) pathology and immune responses were profoundly decreased in CX3CR1-deficient mice and upon blocking CX3CL1-CX3CR1 interactions in wild-type mice. PMID: 24821910
Loss of ACE2 exacerbates AngII-mediated inflammation, myocardial injury and dysfunction in ACE2-deficient hearts via activation of the CTGF-FKN-ERK and MMP signaling. PMID: 24161906
CX3CL1 transiently potentiates NMDAR function though mechanisms involving A2AR activity and the release of D-serine. PMID: 23981568
Interactions between CX3CL1 and CX3CR1 may contribute to the development of leukocytoclastic vasculitis. PMID: 23470165
HDACs and NF-kB signaling coordinate epithelial expression of CX3CL1 to promote mucosal antimicrobial defense through suppression of the mir-424-503 gene. PMID: 23724129
carotid artery injury was associated with greater chemokine 1 CX3C expression in the acute phase followed by greater CX3C receptor 1 coexpressing smooth muscle-like cell content in later lesions and less neointima formation than in femoral arteries PMID: 23653073
our data indicate an upregulation of fractalkine and downregulation of CX3CR1 in sepsis, which seems to be mediated by the transcripting factor NF-KappaB likely via reduced liberation of proinflammtory cytokines in the whole murine organism. PMID: 23026294
Extracellular adenosine is an endogenous modulator of neuroinflammation that induces CX3CL1 at the chorid plexus. PMID: 22883932
Fractalkine's essential role in the formation of atherosclerotic lesions and atherosclerosis progression has been impressively described in mouse models. Review. PMID: 22739755
Suggest that Ang-II induces functional CX(3)CL1 expression in arterial but not in venous endothelial cells. PMID: 23117657
H(2)S hampers the progression of atherosclerosis in fat-fed apoE(-/-) mice and downregulates CX3CR1 and CX3CL1 expression on macrophages and in lesion plaques PMID: 22815945
Hypoxic release of endothelial CX3CL1 induced SMC phenotypic switching from the contractile to the proliferative state. Inhibition of CX3CR1 prevented CX3CL1 stimulation of SMC proliferation and monolayer expansion. PMID: 23002075
Fractalkine is expressed in early and advanced atherosclerotic lesions and supports monocyte recruitment via CX3CR1. PMID: 22916279
Fractalkine induced cellular reactive oxygen species production and activation of ERK1/2 and p38 MAPK in mesangial cells, stimulating cell proliferation. PMID: 22564616
Lipopolysaccharide induces monocyte-mesangial cell binding through the fractalkine/CX3CR1 system. PMID: 22564617
findings that exogenous fractalkine reduces microglial motility and fails to protect neurons co-cultured with Cx3cr1-/- mixed glia suggest that fractalkine may act by interfering with toxic microglial-neuron interactions PMID: 22093090
Fractalkine promotes myocardial injury and accelerates the progress of heart failure, which is associated with the activation of MAPKs. PMID: 21840883
Structure/function and expression analysis of the CX3C chemokine fractalkine. PMID: 21951685
fractalkine-CX3CR1 axis contributes to kidney fibrosis in a hypertensive mouse model. PMID: 21451526
Syk mediated chemotaxis toward CX3CL1 by regulating both Rac1/WAVE2 and Cdc42/WASP pathways, whereas Src family kinases were required for proper WASP tyrosine phosphorylation. PMID: 21388954
Fractalkine attenuates excito-neurotoxicity via microglial clearance of damaged neurons and antioxidant enzyme heme oxygenase-1 expression PMID: 21071446
CX3CR1-expressing macrophages are induced by CX3CL1/fractalkine to express heme oxygenase-1, thereby ameliorating Clostridium difficile toxin A-induced enteritis. PMID: 21131421
Fractalkine-induced depression of excitatory postsynaptic current is absent in cultures from adenosine A3 receptor-deficient mice but not in tissue from adenosine A1- or A2-receptor-deficient mice. PMID: 20570369
The CX3CL1-CX3CR1 interaction inhibits inflammatory properties in Kupffer cells/macrophages and results in decreased liver inflammation and fibrosis. PMID: 20683935

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.