TARC/CCL17 Antibody (Rabbit mAb) [P14H22]

Application: Reactivity: Human

Usage Information

Dilution
IHC1:500

Application
IHC

Reactivity
Human

Source
Rabbit 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
11 kDa

Positive Control	Human Hodgkin lymphoma tissue; Human non-Hodgkin lymphoma tissue; Human tonsil tissue
Negative Control

Datasheet & SDS

Biological Description

Specificity
TARC/CCL17 Antibody (Rabbit mAb) [P14H22] detects endogenous levels of total TARC/CCL17 protein.

Clone
P14H22

Synonym(s)
SCYA17, TARC, CCL17, C-C motif chemokine 17, CC chemokine TARC, Small-inducible cytokine A17, Thymus and activation-regulated chemokine

Background
CCL17, originally identified as thymus and activation-regulated chemokine, belongs to the CC chemokine subfamily and was first characterized as a T cell-directed chemokine constitutively expressed in the thymus, with inducible expression in peripheral blood mononuclear cells following mitogen stimulation. CCL17 functions as a highly specific biological ligand for the G-protein-coupled receptor CCR4, and engagement requires two distinct binding sites on the chemokine, since antibody blockade of either site independently disrupts CCR4 signaling and abolishes the establishment of localized inflammatory responses. CCR4 is expressed predominantly on Th2 cells alongside multiple other lymphocyte subsets, including skin-homing T cells bearing cutaneous lymphocyte antigen, regulatory T cells, Th17 and Th22 populations, and CCL17 binding drives directional T cell migration together with intracellular calcium mobilization. Downstream of receptor engagement, phospholipase-C-dependent, calcium-independent mechanisms are required for the directional component of T cell migration, distinguishing the motility-driving signal from the calcium flux that accompanies receptor activation, while pertussis toxin sensitivity across multiple cell systems indicates that heterotrimeric G-protein coupling underlies the chemotactic response. CCR4 also engages β-arrestin following ligand binding, and CCL17 and the related ligand CCL22 differ in the degree of receptor internalization and desensitization they produce, a distinction attributed to CCR4 adopting at least two structurally distinct conformational states that shape how the receptor responds to repeated or combined ligand exposure. Beyond CCR4, CCL17 also signals through CXCR4, activating PI3K, Akt, and ERK pathways that support cytoskeletal reorganization and directional movement in immune cells, extending the chemokine's functional reach beyond its originally described receptor. CCL17 is produced by monocytes and monocyte-derived dendritic cells in response to GM-CSF, IL-3, and IL-4, and epidermal keratinocytes generate CCL17 within lesional skin under stimulation by IFN-gamma, TNF-alpha, and related inflammatory cytokines, positioning local tissue production as the driver of CCR4-positive lymphocyte recruitment into inflamed sites. Serum CCL17 levels track closely with clinical severity in atopic dermatitis and rise in asthmatic airway secretions, reflecting the chemokine's role in sustaining Th2-dominated inflammation in both skin and lung, and CCR4 blockade or CCL17 neutralization reduces disease-associated T cell and eosinophil recruitment in experimental models, establishing the CCL17-CCR4 axis as an active point of therapeutic intervention in allergic and Th2-driven inflammatory disease.

Background

CCL17, originally identified as thymus and activation-regulated chemokine, belongs to the CC chemokine subfamily and was first characterized as a T cell-directed chemokine constitutively expressed in the thymus, with inducible expression in peripheral blood mononuclear cells following mitogen stimulation. CCL17 functions as a highly specific biological ligand for the G-protein-coupled receptor CCR4, and engagement requires two distinct binding sites on the chemokine, since antibody blockade of either site independently disrupts CCR4 signaling and abolishes the establishment of localized inflammatory responses. CCR4 is expressed predominantly on Th2 cells alongside multiple other lymphocyte subsets, including skin-homing T cells bearing cutaneous lymphocyte antigen, regulatory T cells, Th17 and Th22 populations, and CCL17 binding drives directional T cell migration together with intracellular calcium mobilization. Downstream of receptor engagement, phospholipase-C-dependent, calcium-independent mechanisms are required for the directional component of T cell migration, distinguishing the motility-driving signal from the calcium flux that accompanies receptor activation, while pertussis toxin sensitivity across multiple cell systems indicates that heterotrimeric G-protein coupling underlies the chemotactic response. CCR4 also engages β-arrestin following ligand binding, and CCL17 and the related ligand CCL22 differ in the degree of receptor internalization and desensitization they produce, a distinction attributed to CCR4 adopting at least two structurally distinct conformational states that shape how the receptor responds to repeated or combined ligand exposure. Beyond CCR4, CCL17 also signals through CXCR4, activating PI3K, Akt, and ERK pathways that support cytoskeletal reorganization and directional movement in immune cells, extending the chemokine's functional reach beyond its originally described receptor. CCL17 is produced by monocytes and monocyte-derived dendritic cells in response to GM-CSF, IL-3, and IL-4, and epidermal keratinocytes generate CCL17 within lesional skin under stimulation by IFN-gamma, TNF-alpha, and related inflammatory cytokines, positioning local tissue production as the driver of CCR4-positive lymphocyte recruitment into inflamed sites. Serum CCL17 levels track closely with clinical severity in atopic dermatitis and rise in asthmatic airway secretions, reflecting the chemokine's role in sustaining Th2-dominated inflammation in both skin and lung, and CCR4 blockade or CCL17 neutralization reduces disease-associated T cell and eosinophil recruitment in experimental models, establishing the CCL17-CCR4 axis as an active point of therapeutic intervention in allergic and Th2-driven inflammatory disease.

References
https://pubmed.ncbi.nlm.nih.gov/16859899/ https://pubmed.ncbi.nlm.nih.gov/41291326/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

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%