CCL5/RANTES Antibody (Mouse mAb) [K11A8]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IHC1:20-1:125 FCM1:4000

Application
WB, IHC, FCM

Reactivity
Human

Source
Mouse Monoclonal Antibody

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

Predicted MW
10 kDa

Positive Control	Mouse small intestine
Negative Control

Datasheet & SDS

Biological Description

Specificity
CCL5/RANTES Antibody (Mouse mAb) [K11A8] detects endogenous levels of total CCL5/RANTES protein.

Clone
K11A8

Synonym(s)
C-C motif chemokine 5, EoCP, Eosinophil chemotactic cytokine, SIS-delta, Small-inducible cytokine A5, T cell-specific protein P228 (TCP228), T-cell-specific protein RANTES, CCL5, D17S136E, SCYA5

Background
CCL5, originally named RANTES for Regulated upon Activation, Normal T cell Expressed and presumably Secreted, belongs to the CC subfamily of chemokines and signals through three G-protein-coupled receptors, CCR1, CCR3, and CCR5, with CCR5 representing its primary and most extensively characterized receptor partner. CCL5 assembles from a canonical CC-chemokine dimer into higher-order, rod-shaped double-helical oligomers through a polymerization mechanism, and this oligomerization is coupled to binding of glycosaminoglycans on cell surfaces and in the extracellular matrix, with a positively charged, fully exposed KKWVR motif mediating the GAG interaction distinct from the buried BBXB motifs used by related chemokines such as CCL3. Mutations that disrupt key residues involved in dimer-dimer contacts, including E66 and E26, produce a disaggregating effect on CCL5 oligomers, directly linking specific charged residues to the higher-order assembly process rather than to receptor engagement itself. This oligomerization and GAG-binding activity is functionally required rather than incidental: CCR1-mediated arrest of leukocytes on inflamed endothelium depends specifically on CCL5 oligomerization, whereas CCR5-mediated transmigration of leukocytes proceeds independently of oligomer formation, showing that the two receptors engage functionally distinct forms of the chemokine to produce different steps of the leukocyte adhesion cascade. Receptor engagement by CCL5 induces a conformational change in CCR5 that activates heterotrimeric G-protein subunits, triggering changes in cyclic AMP, inositol triphosphate, and intracellular calcium alongside tyrosine kinase activation, and these signaling events drive cell polarization and translocation of NF-κB, increasing phagocytic capacity, cell survival, and transcription of proinflammatory genes. CCL5 also forms heterooligomers with other chemokines such as CXCL4, particularly when CXCL4 is present in excess following platelet activation, and this heterooligomer complex alters the surface charge distribution of the assembly, allowing tighter GAG binding than CCL5 oligomers formed alone, extending CCL5's functional repertoire beyond homotypic self-assembly. In the tumor microenvironment, CCL5-CCR5 signaling recruits regulatory T cells and myeloid-derived suppressor cells, polarizes tumor-associated macrophages, supports epithelial-mesenchymal transition, and stabilizes PD-L1 expression, connecting the same oligomerization- and GAG-dependent mechanisms established in inflammatory contexts to protumorigenic processes and therapeutic resistance. CCL5 additionally contributes to fibrosis progression through CCR1 and CCR5 signaling in experimental liver injury models, where receptor antagonism ameliorates fibrotic scarring, underscoring the CCL5-CCR1/CCR5 axis as a defined target across inflammatory, fibrotic, and oncological disease contexts.

Background

CCL5, originally named RANTES for Regulated upon Activation, Normal T cell Expressed and presumably Secreted, belongs to the CC subfamily of chemokines and signals through three G-protein-coupled receptors, CCR1, CCR3, and CCR5, with CCR5 representing its primary and most extensively characterized receptor partner. CCL5 assembles from a canonical CC-chemokine dimer into higher-order, rod-shaped double-helical oligomers through a polymerization mechanism, and this oligomerization is coupled to binding of glycosaminoglycans on cell surfaces and in the extracellular matrix, with a positively charged, fully exposed KKWVR motif mediating the GAG interaction distinct from the buried BBXB motifs used by related chemokines such as CCL3. Mutations that disrupt key residues involved in dimer-dimer contacts, including E66 and E26, produce a disaggregating effect on CCL5 oligomers, directly linking specific charged residues to the higher-order assembly process rather than to receptor engagement itself. This oligomerization and GAG-binding activity is functionally required rather than incidental: CCR1-mediated arrest of leukocytes on inflamed endothelium depends specifically on CCL5 oligomerization, whereas CCR5-mediated transmigration of leukocytes proceeds independently of oligomer formation, showing that the two receptors engage functionally distinct forms of the chemokine to produce different steps of the leukocyte adhesion cascade. Receptor engagement by CCL5 induces a conformational change in CCR5 that activates heterotrimeric G-protein subunits, triggering changes in cyclic AMP, inositol triphosphate, and intracellular calcium alongside tyrosine kinase activation, and these signaling events drive cell polarization and translocation of NF-κB, increasing phagocytic capacity, cell survival, and transcription of proinflammatory genes. CCL5 also forms heterooligomers with other chemokines such as CXCL4, particularly when CXCL4 is present in excess following platelet activation, and this heterooligomer complex alters the surface charge distribution of the assembly, allowing tighter GAG binding than CCL5 oligomers formed alone, extending CCL5's functional repertoire beyond homotypic self-assembly. In the tumor microenvironment, CCL5-CCR5 signaling recruits regulatory T cells and myeloid-derived suppressor cells, polarizes tumor-associated macrophages, supports epithelial-mesenchymal transition, and stabilizes PD-L1 expression, connecting the same oligomerization- and GAG-dependent mechanisms established in inflammatory contexts to protumorigenic processes and therapeutic resistance. CCL5 additionally contributes to fibrosis progression through CCR1 and CCR5 signaling in experimental liver injury models, where receptor antagonism ameliorates fibrotic scarring, underscoring the CCL5-CCR1/CCR5 axis as a defined target across inflammatory, fibrotic, and oncological disease contexts.

References
https://pubmed.ncbi.nlm.nih.gov/27091995/ https://pubmed.ncbi.nlm.nih.gov/40976299/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%