Product Sheet CG1678
Description
BACKGROUND family of chemoattractant molecules involved in the directed migration of immune cells. Over fifty human chemokines have been identified that can be categorised into four groups; CC, CXC, CX3C and C (XCL1 and XCL2); depending on the spacing of their first two cysteine residues. Chemokines exert their effects by binding to G-protein-coupled chemokine receptors on the surface of cells, predominantly leukocytes. Eighteen human chemokine receptors have been identified that are classified according to the class of chemokines that they bind.1 The major function of chemokines is to regulate leukocyte trafficking in hematopoiesis and in innate and adaptive immunity. Other functions include angiogenic activity, apoptosis, T-cell differentiation and phagocyte activation. Inadvertent activation of chemokine receptors leads to autoimmunity by inappropriately targeting self antigens for destruction by cytotoxic T-cells and macrophages.2
CCR7 is a member of the G protein-coupled receptor family. This receptor was identified as a gene induced by the Epstein-Barr virus (EBV), and is thought to be a mediator of EBV effects on B lymphocytes. This receptor is expressed in various lymphoid tissues and activates B and T lymphocytes. It has been shown to control the migration of memory T cells to inflamed tissues, as well as stimulate dendritic cell maturation. The chemokine (C-C motif) ligand 19 (CCL19/ECL) has been reported to be a specific ligand of this receptor.3
CCR7 is a member of the G protein-coupled receptor family. This receptor was identified as a gene induced by the Epstein-Barr virus (EBV), and is thought to be a mediator of EBV effects on B lymphocytes. This receptor is expressed in various lymphoid tissues and activates B and T lymphocytes. It has been shown to control the migration of memory T cells to inflamed tissues, as well as stimulate dendritic cell maturation. The chemokine (C-C motif) ligand 19 (CCL19/ECL) has been reported to be a specific ligand of this receptor.3
REFERENCES
1. Zlotnik, A. & Yoshie, O.:Immunity 12:121-27, 2000
2. Locati, M.: Ann. Rev. Med. 50:425-40, 1999
3. Forster, R. et al: Cell 99:23-33, 1999
2. Locati, M.: Ann. Rev. Med. 50:425-40, 1999
3. Forster, R. et al: Cell 99:23-33, 1999
Products are for research use only. They are not intended for human, animal, or diagnostic applications.
(Click to Enlarge)
Top: Immunoblotting analysis of extracts from COS7 cells, using Anti-CCR7 antibody. The lane on the left was treated with the Anti-CCR7 antibody. The lane on the right (negative control) was treated with both Anti-CCR7 antibody and the synthesized immunogen peptide. Bottom: Immunofluorescence of A549 cells using Anti-CCR7 antibody. Cells on the left were treated with the Anti-CCR7 antibody. Cells on the right (negative control) were treated with both Anti-CCR7 antibody and the synthesized immunogen peptide.
Details
Cat.No.: | CG1678 |
Antigen: | Synthesized peptide derived from human CCR7. |
Isotype: | Rabbit IgG |
Species & predicted species cross- reactivity ( ): | Human |
Applications & Suggested starting dilutions:* | WB 1:500-1:1000 IP n/d IHC n/d ICC n/d FACS n/d IF 1:100-1:500 |
Predicted Molecular Weight of protein: | 42 kDa |
Specificity/Sensitivity: | Detects endogenous CCR7 proteins without cross-reactivity with other family members. |
Storage: | Store at -20°C, 4°C for frequent use. Avoid repeated freeze-thaw cycles. |
*Optimal working dilutions must be determined by end user.
Products
| Product | Size | CAT.# | Price | Quantity |
|---|---|---|---|---|
| Rabbit CCR7 Antibody: Rabbit CCR7 Antibody | Size: 100 ul | CAT.#: CG1678 | Price: $384.00 |
Resources/Documents
Publications
2012
Tous, E., H. Weber, M. Lee, K. Koomalsingh, T. Shuto, N. Kondo, J. Gorman, D. Lee, R. Gorman, and J. Burdick. 2012. Tunable hydrogel-microsphere composites that modulate local inflammation and collagen bulking. Acta Biomateriala, 8:3218-3227.
2009
Triana-Baltzer, G.B., L.V. Gubareva, J.M. Nicholls, M.B. Pearce, V.P. Mishin, J.A. Belser, L.-M. Chen, R.W.Y. Chan, M.C.W. Chan, M. Hedlund, J.L. Larson, R.B. Moss, J.M. Katz, T.M. Valentin, J. 2009. MACROPHAGE INVOLVEMENT IN THE REMODELING OF AN EXTRACELLULAR MATRIX SCAFFOLD. PhD Dissertation, U Pittsburgh.