Catalog number: 209 - 101-M271
Product Category: Business & Industrial > Science & Laboratory
Size: 100 µg
101-M271
CTACK or CCL-27 is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant human CTACK is a 10.2 kDa protein containing 88 amino acid residues.
101-M184
CTACK or CCL-27 is a keratinocyte-derived CC chemokine which signals through the CCR10 receptor. Both CTACK and CCR10 are expressed in normal and irritated epithelial cells. CTACK selectively attracts CLA+ T-cells and directs them into the skin. CTACK contains the four highly conserved cysteine residues present in most CC chemokines. The mature protein contains 88 amino acid residues. Recombinant human CTACK is a 10.2 kDa protein containing 88 amino acid residues.
103-M331
CCL27, also known as CTACK (cutaneous T cel-lattracting chemokine), ALP, ILC, and ESkine, is a member of the CC family of chemokines. Mature mouse CCL27 is a 95 amino acid (aa) protein that shares 57% aa and 87% aa sequence identity with human and rat CCL27, respectively. It shares 18-31% aa sequence identity with other mouse CC chemokines. An alternately spliced form of mouse CCL27, known as PESKY, is localized to the nucleus and promotes cellular migration. CCL27 is constitutively expressed by keratinocytes and is upregulated by inflammatory stimuli and in wounded skin. CCL27 binds the chemokine receptor CCR10, glycosaminoglycans in the extracellular matrix, sulfated tyrosine residues on PSGL1, and determinants on the surface of fibroblasts and endothelial cells. CCL27 cooperates with CCL17/TARC in inducing the migration of cutaneous lymphocyte antigen (CLA) positive memory T cells to the skin during inflammation. Endothelial cellbound CCL27 can mediate the adhesion of those cells to CLA+ T cells. CCL27 also induces the migration of keratinocyte precursors from bone marrow to the skin, thereby promoting wound healing. In humans, serum CCL27 levels are elevated and correlate with disease severity in atopic dermatitis, psoriasis vulgaris, and mycosis fungoides.
103-M327
6Ckine is a novel CC chemokine discovered independently by three groups from the EST database. 6Ckine, also named SLC (secondary lymphoidtissue chemokine), CCL21 and Exodus2, shows 21-33% identity to other CC chemokines. 6Ckine contains the four conserved cysteines characteristic of β chemokines plus two additional cysteines in its unusually long carboxy-lterminal domain. Human 6Ckine cDNA encodes a 134 amino acid highly basic precursor protein with a 23 amino acid residue signal peptide that is cleaved to form the predicted 111 amino acid residue mature protein. Mouse 6Ckine cDNA encodes a 133 amino acid residue protein with a 23 residue signal peptide that is cleaved to generate the 110 residue mature protein. Human and mouse 6Ckine share 86% amino acid sequence identity. 6Ckine is constitutively expressed at high levels in lymphoid tissues such as lymph nodes, spleen and appendix. In mouse, high levels of 6Ckine mRNA are also detected in the lung. Unlike most CC chemokines, 6Ckine is not chemotactic for monocytes. Recombinant mouse 6Ckine is chemotactic in vitro for thymocytes and activated T cells. Recombinant human 6Ckine has been shown to be chemotactic for some human T cell lines, resting PBL, and cultured T cells expanded with PHA and IL2. 6Ckine has also been reported to inhibit hemopoietic progenitor colony formation in a dosedependent manner. 6Ckine acts via the CC receptor CCR7 on T cells and B cells.
103-M328
CCL22, also known as ABCD1 and MDC (macrophage-derived chemokine), is a CC chemokine cloned from activated mouse B cells. Mouse CCL22 cDNA encodes a precursor protein of 92 amino acid (aa) residues with a 24 aa residue predicted signal peptide that is cleaved to yield a 68 aa residue mature 7.8 kDa protein. At the amino acid sequence level, mouse and human CCL22 share 64% identity and 83% similarity. The genomic organization of the mouse and human CCL22 genes are very similar, exhibiting sequence identity at the intron-exon boundaries. Mouse CCL22 is expressed at high levels in dendritic cells and activated B lymphocytes. Low levels of mouse CCL22 mRNA are also detectable in lung, unstimulated spleen cells, lymph node cells and in thymocytes. CCL22 is a functional ligand for the CC chemokine receptor 4. Recombinant or chemically synthesized mature mouse CCL22 has been shown to induce chemotaxis or Ca2+ mobilization in activated mouse and human T cells.
103-M329
Eotaxin2, also named myeloid progenitor inhibitory factor (MPIF2), is a member of the CC chemokine subfamily and is designated CCL24. Eotaxin2 is constitutively expressed in the jejunum and spleen. It can also be induced in the lung by allergen challenge and IL4. LPS and IL4 also differentially regulate the expression of Eotaxin2 in monocytes and macrophages. Mouse Eotaxin2 cDNA encodes a 119 amino acid (aa) precursor protein that shares approximately 58% aa sequence identity with human Eotaxin2. Functionally, Eotaxin2is most closely related to CCL11/Eotaxin and CCL26/Eotaxin3. The three proteins share low sequence homology but have been shown to be potent eosinophil chemoattractants that bind and activate the chemokine receptor CCR3, a receptor that is highly expressed in eosinophils. Eotaxin2 also has the ability to suppress myeloid cell proliferation, a biological function not shared by Eotaxin.