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anti-Human RARRES2 Antikörper:
anti-Mouse (Murine) RARRES2 Antikörper:
anti-Rat (Rattus) RARRES2 Antikörper:
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Mouse (Murine) Polyclonal RARRES2 Primary Antibody für IF (cc), IF (p) - ABIN1715135
Krautbauer, Wanninger, Eisinger, Hader, Beck, Kopp, Schmid, Weiss, Dorn, Buechler: Chemerin is highly expressed in hepatocytes and is induced in non-alcoholic steatohepatitis liver. in Experimental and molecular pathology 2013
Show all 3 Pubmed References
Mouse (Murine) Polyclonal RARRES2 Primary Antibody für IHC (p) - ABIN1701633
Gonzalvo-Feo, Del Prete, Pruenster, Salvi, Wang, Sironi, Bierschenk, Sperandio, Vecchi, Sozzani: Endothelial cell-derived chemerin promotes dendritic cell transmigration. in Journal of immunology (Baltimore, Md. : 1950) 2014
Suggest chemerin is a major factor in the secretome of senescent fibroblasts, promoting cutaneous squamous carcinoma cell migration, and possibly progression, relaying its signals through CCRL2 (zeige CCRL2 Antikörper) and GPR1 (zeige GPR1 Antikörper) receptors with subsequent MAPK (zeige MAPK1 Antikörper) activation.
Data suggest that chemerin acts at CMKLR1 (zeige CMKLR1 Antikörper), but not GPR1 (zeige GPR1 Antikörper), to increase blood pressure. Chemerin is expressed in vascular endothelium, smooth muscle, and adventitia.
Data suggest that primary cells from papillary renal cell carcinoma (zeige MOK Antikörper) secrete the chemokines IL8 (zeige IL8 Antikörper), CXCL16 (zeige CXCL16 Antikörper), and chemerin; these chemokines attract primary human monocytes and induce shift/transdifferentiation in monocytes toward M2 macrophage/foam cell phenotype. (IL8 (zeige IL8 Antikörper) = interleukin-8 (zeige IL8 Antikörper); CXCL16 (zeige CXCL16 Antikörper) = C-X-C motif chemokine (zeige CCL1 Antikörper) ligand 16)
Chemerin-CMKLR1 (zeige CMKLR1 Antikörper) activates Akt (zeige AKT1 Antikörper)/mTOR (zeige FRAP1 Antikörper) and ERK (zeige EPHB2 Antikörper) pathways and facilitates preadipocyte proliferation, adipogenesis, and angiogenesis. Gax (zeige MEOX2 Antikörper) weakens the effect of chemerin on preadipocyte biofunctions.
RARRES2 overexpression in adrenocortical carcinoma cells inhibited Wnt (zeige WNT2 Antikörper)/beta-catenin (zeige CTNNB1 Antikörper) pathway activity by promoting beta-catenin (zeige CTNNB1 Antikörper) phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase (zeige MAPK14 Antikörper). Thus our study identifies RARRES2 as a novel tumor suppressor for adrenocortical carcinoma, which can function through an immune-independent mechanism.
study reveals the tumor-inhibitory effect of chemerin by suppressing inflammatory tumor microenvironment with therapeutic implications for inflammation-associated cancer-like Hepatocellular carcinoma.
Further analysis of chemerin functions in vivo might constitute a crucial step toward optimizing Mesenchymal stromal cells-based therapy for inflammatory diseases.
Stimulation of mesenchymal stromal cells (MSCs) by chemerin increases phosphorylation of p42 (zeige EPB42 Antikörper)/44, p38 (zeige CRK Antikörper) and JNK (zeige MAPK8 Antikörper)-II kinases and inhibitors of these kinases and PKC (zeige PRRT2 Antikörper) reverse chemerin-stimulated MSC (zeige MSC Antikörper) migration.
Elevated chemerin levels in colons from ulcerative colitis patients correlate with disease severity
cathepsin S (zeige CTSS Antikörper) and chemerin only correlated positively with insulin (zeige INS Antikörper) resistance and inflammation
endogenously secreted chemerin plays an autocrine/paracrine role in white adipose tissue, identifying chemerin as a therapeutic target to modulate adipose remodelling.
elevated levels of chemerin were found in colons of mice with experimental colitis, and a neutralizing anti-chemerin antibody improved intestinal inflammation
Data suggest a potential role for chemerin and CMKLR1 (zeige CMKLR1 Antikörper) in the regulation of inflammatory responses in the tumor microenvironment.
Suggest reduction of chemerin could contribute to the antiobesity/antidiabetic properties described for alpha-lipoic acid.
Study indicates that Chemerin plays a role in the negative cross-talk between skeletal muscle and adipose tissue. Specifically, Chemerin promotes the adipogenic differentiation potential and alters the myoblast cell fate from myogenesis to adipogenesis.
Data indicate that chemerin may play an important role in regulating mitochondrial remodelling and function in skeletal muscle.
The chemerin15 (C15) precursor, chemerin, and its receptor, ChemR23, are both upregulated after skin damage and the receptor is expressed by macrophages, neutrophils, and keratinocytes. C15 delivery dampens immediate inflammatory events.
findings reveal previously uncharacterized regulators of chemerin expression in skin and identify a physiologic role for chemerin in skin barrier defense against microbial pathogens.
A novel autocrine/paracrine role for chemerin in regulating osteoclast differentiation of hematopoietic stem cells
this study reports that retinoic acid-activated endothelial cells can promote myeloid and plasmacytoid dendritic cell transmigration across endothelial cell monolayers through the endogenous production of chemerin
Chemerin regulates energy metabolism partly through the Akt (zeige AKT1 Antikörper) and ERK1/2 (zeige MAPK1/3 Antikörper) signaling pathways.
These results suggest that Chemerin promotes lipolysis in mature adipocytes and induces adipogenesis during preadipocyte re-differentiation, further indicating a dual role for Chemerin in the deposition of intramuscular fat in ruminant animals.
chemerin is a novel regulator of lactogenesis via its own receptor in bovine mammary epithelial cells
This gene encodes a secreted chemotactic protein that initiates chemotaxis via the ChemR23 G protein-coupled seven-transmembrane domain ligand. Expression of this gene is upregulated by the synthetic retinoid tazarotene and occurs in a wide variety of tissues. The active protein has several roles, including that as an adipokine, and is truncated on both termini from the proprotein.
RAR-responsive protein TIG2
, retinoic acid receptor responder protein 2
, tazarotene-induced gene 2 protein
, CHO functionally unknown type II transmembrane protein
, Tazarotene-induced gene 2 protein