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anti-Human RARRES2 Antibodies:
anti-Mouse (Murine) RARRES2 Antibodies:
anti-Rat (Rattus) RARRES2 Antibodies:
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Mouse (Murine) Polyclonal RARRES2 Primary Antibody for 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 for 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
High chemerin expression is associated with metabolic complications.
results show that chemerin not only increases osteoclasts activity in vitro, but also that increased level of chemerin in dyslipidemic mice plays a critical role in bone homeostasis.
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 (show CCRL2 Antibodies) and GPR1 (show GPR1 Antibodies) receptors with subsequent MAPK (show MAPK1 Antibodies) activation.
Data suggest that chemerin acts at CMKLR1 (show CMKLR1 Antibodies), but not GPR1 (show GPR1 Antibodies), to increase blood pressure. Chemerin is expressed in vascular endothelium, smooth muscle, and adventitia.
Data suggest that primary cells from papillary renal cell carcinoma (show MOK Antibodies) secrete the chemokines IL8 (show IL8 Antibodies), CXCL16 (show CXCL16 Antibodies), and chemerin; these chemokines attract primary human monocytes and induce shift/transdifferentiation in monocytes toward M2 macrophage/foam cell phenotype. (IL8 (show IL8 Antibodies) = interleukin-8 (show IL8 Antibodies); CXCL16 (show CXCL16 Antibodies) = C-X-C motif chemokine (show CCL1 Antibodies) ligand 16)
Chemerin-CMKLR1 (show CMKLR1 Antibodies) activates Akt (show AKT1 Antibodies)/mTOR (show FRAP1 Antibodies) and ERK (show EPHB2 Antibodies) pathways and facilitates preadipocyte proliferation, adipogenesis, and angiogenesis. Gax (show MEOX2 Antibodies) weakens the effect of chemerin on preadipocyte biofunctions.
RARRES2 overexpression in adrenocortical carcinoma cells inhibited Wnt (show WNT2 Antibodies)/beta-catenin (show CTNNB1 Antibodies) pathway activity by promoting beta-catenin (show CTNNB1 Antibodies) phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase (show MAPK14 Antibodies). 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 (show EPB42 Antibodies)/44, p38 (show CRK Antibodies) and JNK (show MAPK8 Antibodies)-II kinases and inhibitors of these kinases and PKC (show PRRT2 Antibodies) reverse chemerin-stimulated MSC (show MSC Antibodies) migration.
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 (show CMKLR1 Antibodies) 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 and ERK1/2 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