Recombinant Human Retinoic Acid Receptor Responder Protein 2 (RARRES2) Protein (His-SUMO)

Name: Recombinant Human Retinoic Acid Receptor Responder Protein 2 (RARRES2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03187P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Retinoic Acid Receptor Responder Protein 2 (RARRES2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q99969
Target Symbol	RARRES2
Synonyms	HP10433; RAR responsive protein TIG2; RAR-responsive protein TIG2; RARR2_HUMAN; RARRES2; Retinoic acid receptor responder (tazarotene induced) 2; Retinoic acid receptor responder 2; Retinoic acid receptor responder protein 2; Tazarotene induced gene 2 protein; Tazarotene-induced gene 2 protein; TIG2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	ELTEAQRRGLQVALEEFHKHPPVQWAFQETSVESAVDTPFPAGIFVRLEFKLQQTSCRKRDWKKPECKVRPNGRKRKCLACIKLGSEDKVLGRLVHCPIETQVLREAEEHQETQCLRVQRAGEDPHSFYFPGQFAFS
Expression Range	21-157aa
Protein Length	Full Length of Mature Protein
Mol. Weight	31.9kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Acts also as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2. Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a proinflammatory adipokine, causing an increase in secretion of proinflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin.
Subcellular Location	Secreted.
Database References	HGNC: 9868 OMIM: 601973 KEGG: hsa:5919 STRING: 9606.ENSP00000223271 UniGene: PMID: 29337272 The elevated levels of circulating TIG2 (chemerin) were associated with gestational diabetes mellitus.[meta-analysis] PMID: 30041634 This study show the serum PARRES2 levels had significant positive correlation with seizure severity Chalfont score and the duration of epilepsy. PMID: 29860632 findings of this study suggest that chemerin in synovial fluid may play role as a predisposing factor and may represent a novel potential prognostic biochemical marker in the pathogenesis of temporomandibular joint disorders PMID: 29331039 G allele of chemerin rs17173608 compared to T allele decreased the risk of end-stage renal disease in a sample of Iranian population. PMID: 29644922 Data suggest that down-regulation of serum levels of chemerin (an inflammatory cytokine biomarker) can occur in weight-loss therapy as short in duration as 4-week aerobic exercise plus dieting in obese female adolescents; this effect was not observed by dieting alone. This study was conducted in weight-loss summer camp in China. PMID: 29306931 results demonstrate a strong inverse association between serum chemerin levels and renal function. PMID: 28833355 The aims of this study were to evaluate and correlate circulating chemerin, apelin, vaspin, and omentin-1 levels in obese type 2 diabetic Egyptian patients with coronary artery stenosis (CAS), and to assess their usefulness as noninvasive diagnostic biomarkers. PMID: 28957639 Data suggest that, in overweight and obese subjects, weight reduction induces changes in chemerin serum levels in parallel with adiponectin plasma levels; chemerin is down-regulated and adiponectin is up-regulated in both insulin-resistant and insulin-sensitive subjects after weight reduction; however, only changes in chemerin in insulin-sensitive subjects were found to be statistically significant. PMID: 28323510 No associations were observed between SNPs in RARRES2 and obesity. PMID: 28947843 Serum chemerin level during the first trimester of pregnancy has the potential to predict risk of gestational diabetes mellitus. PMID: 28454507 The SD to LD transition was mimicked by 2 weeks of ICV infusion of human chemerin into rats. It also increased expression of the cytoskeletal protein vimentin, implicating hypothalamic remodeling in this response.Acute ICV bolus injection of chemerin on a 12 h:12 h photoperiod inhibited food intake and decreased body weight with associated changes in hypothalamic neuropeptides involved in growth and feeding after 24 hr. PMID: 27225311 We studied the association between retinoic acid receptor responder 2 rs17173608 and rs4721 gene polymorphisms and gestational diabetes mellitus. We found that RARRES2 rs4721 polymorphism increased the risk of gestational diabetes mellitus. RARRES2 rs17173608 polymorphism is not associated with gestational diabetes mellitus. PMID: 29360607 High chemerin expression is associated with metabolic complications. PMID: 28551507 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. PMID: 28029186 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 and GPR1 receptors with subsequent MAPK activation. PMID: 27907906 Data suggest that chemerin acts at CMKLR1, but not GPR1, to increase blood pressure. Chemerin is expressed in vascular endothelium, smooth muscle, and adventitia. PMID: 27742615 Data suggest that primary cells from papillary renal cell carcinoma secrete the chemokines IL8, CXCL16, and chemerin; these chemokines attract primary human monocytes and induce shift/transdifferentiation in monocytes toward M2 macrophage/foam cell phenotype. (IL8 = interleukin-8; CXCL16 = C-X-C motif chemokine ligand 16) PMID: 28759013 Chemerin-CMKLR1 activates Akt/mTOR and ERK pathways and facilitates preadipocyte proliferation, adipogenesis, and angiogenesis. Gax weakens the effect of chemerin on preadipocyte biofunctions. PMID: 28326537 study reveals the tumor-inhibitory effect of chemerin by suppressing inflammatory tumor microenvironment with therapeutic implications for inflammation-associated cancer-like Hepatocellular carcinoma. PMID: 28166197 Further analysis of chemerin functions in vivo might constitute a crucial step toward optimizing Mesenchymal stromal cells-based therapy for inflammatory diseases. PMID: 27939374 Stimulation of mesenchymal stromal cells (MSCs) by chemerin increases phosphorylation of p42/44, p38 and JNK-II kinases and inhibitors of these kinases and PKC reverse chemerin-stimulated MSC migration. PMID: 25127029 Elevated chemerin levels in colons from ulcerative colitis patients correlate with disease severity PMID: 24727542 cathepsin S and chemerin only correlated positively with insulin resistance and inflammation PMID: 24390241 Cathepsin L- and K-cleaved chemerin trigger robust migration of human blood-derived plasmacytoid dendritic cells ex vivo PMID: 21715684 Plasma chemerin levels are correlated with obesity, blood pressure, and high-density lipoprotein cholesterol, suggesting that it may play a role in the pathogenesis of metabolic syndrome. PMID: 24338392 High serum RARRES2 expression is associated with Adrenocortical Carcinoma. PMID: 27336360 Hypoxia-induced chemerin expression is mediated by TNF-alpha and at least in part by the ERK pathway PMID: 27792771 Low chemerin and high resistin levels were associated with carotid disease severity, suggesting that these adipokines may act as potential markers for plaque instability and stroke risk. PMID: 27312219 Serum chemerin concentrations are associated with the presence of atrial fibrillation and atrial remodeling. PMID: 27496791 Chemerin mRNA is reduced in the liver of nonalcoholic steatohepatitis patients. PMID: 27797398 Results show that chemerin stimulates the migration, invasion and proliferation of oesophageal cancer cells by a pathway sensitive to the ChemR23 antagonist CCX832. PMID: 27092781 In type 2 diabetes mellitus, both chemerin and omentin enhance the body sensitivity to insulin, which results in increased glucose uptake PMID: 27516571 High chemerin expression is associated with Overweight/obese. PMID: 27941174 Circulating levels of the adipokine chemerin are elevated in lipodystrophy, as well as independently and positively associated with HbA1c and CRP. PMID: 26572532 There was no difference in serum chemerin, vaspin and omentin-1 between polycystic ovary syndrome patients and healthy controls. PMID: 27225862 Study demonstrated that circulating chemerin plasma levels are high in patients with chronic obstructive pulmonary disease. PMID: 24865134 We conclude that LDL apheresis decreases the circulating level of chemerin by binding the protein to the column and thus improves lipoprotein subfraction pattern. PMID: 27756331 The production of the two adipokines, chemerin and RBP-4, is strongly associated with obesity in patients with NAFLD. PMID: 27740519 this study suggested that a role of STRA6 polymorphism could also be of value in predicting the risk of type 2 diabetes mellitus(T2DM) while RARRES2 polymorphism could not predict the risk of T2DM. PMID: 27446956 Studied levels of salivary visfatin, chemerin, and progranulin and in gingivitis, periodontitis, as well as healthy patients. Salivary progranulin levels were similar in all groups; chemerin was detected at higher levels in the periodontitis group compared to the gingivitis and the healthy groups; visfatin levels were higher in patients with gingivitis and periodontitis compared to those of healthy subjects. PMID: 25164155 Data show inverse Relationship of the CMKLR1 Relative Expression and Chemerin Serum Levels in Obesity with Dysmetabolic Phenotype and Insulin Resistance PMID: 27239101 Oral lipid loading is linked to reduced circulating pro-inflammatory chemokines CCL2, IP-10, and chemerin and to increased RANTES levels, suggesting that dietary lipids affect immune function. PMID: 26950614 Metabolic syndrome in Egyptian females is associated with the minor allele of chemerin rs17173608 polymorphism. PMID: 26472663 Serum chemerin was significantly higher in the obese PCOS group compared with non-obese PCOS and the obese and non-obese control groups. PMID: 26291816 The synovial fluid and synovial membrane levels of chemerin are increased in knee osteoarthritis patients PMID: 26722546 Together, these findings suggest that CCL2, RARRES2 and EFNB2 are host cell factors involved in respiratory syncytial virus replication. PMID: 26277777 serum chemerin may have a role in acute ischemic stroke and carotid artery plaque instability in Chinese populations PMID: 26471865 Suggest reduction of chemerin could contribute to the antiobesity/antidiabetic properties described for alpha-lipoic acid. PMID: 26721419 chemerin is a novel biomarker of dilated cardiomyopathy PMID: 26057200

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

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