Recombinant Mouse Apelin Receptor (APLNR) Protein (His&Myc)

Name: Recombinant Mouse Apelin Receptor (APLNR) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07787P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Apelin Receptor (APLNR) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9WV08
Target Symbol	APLNR
Synonyms	Aplnr; Agtrl1; Apj; Apelin receptor; Angiotensin receptor-like 1; G-protein coupled receptor APJ; MSR
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	YAFFDPRFRQACTSMLCCDQSGCKGTPHSSSAEKSASYSSGHSQGPGPNMGKGGEQMHEKSIPYSQETLVD
Expression Range	307-377aa
Protein Length	Partial
Mol. Weight	15.1 kDa
Research Area	Cardiovascular
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	Receptor for apelin receptor early endogenous ligand (APELA) and apelin (APLN) hormones coupled to G proteins that inhibit adenylate cyclase activity. Plays a key role in early development such as gastrulation, blood vessels formation and heart morphogenesis by acting as a receptor for APELA hormone. May promote angioblast migration toward the embryonic midline, i.e. the position of the future vessel formation, during vasculogenesis. Promotes sinus venosus (SV)-derived endothelial cells migration into the developing heart to promote coronary blood vessel development. Plays also a role in various processes in adults such as regulation of blood vessel formation, blood pressure, heart contractility and heart failure.
Subcellular Location	Cell membrane; Multi-pass membrane protein.
Protein Families	G-protein coupled receptor 1 family
Database References	KEGG: mmu:23796 STRING: 10090.ENSMUSP00000053638 UniGene: PMID: 28904225 The ELA-APJ axis protects from pressure overload-induced heart failure possibly via suppression of ACE expression and pathogenic angiotensin II signaling. PMID: 28371822 Internalization does not appear to contribute to the desensitization of APJ-mediated ppERK1/2 activation. PMID: 27492965 the ELABELA (ELA)-APJ signaling axis is only required for sinus venosus-derived progenitors. PMID: 28890073 These results demonstrate a new pharmacologic property of protamine-blockade of APJ-that could explain some adverse effects observed in protamine-treated patients, and that the established antiangiogenic activity of protamine would rely on APJ antagonism. PMID: 28242772 Apelin-36-[L28C(30kDa-PEG)] provides a starting point for the development of diabetes therapeutics that are devoid of the blood pressure effects associated with canonical APJ activation PMID: 27994053 Results show that obese mice had significantly lower mRNA and protein expressions of apelin/ APJ in skeletal muscles than the normal body weight mice. PMID: 27834140 These results demonstrate that overexpression of APJ in cardiomyocytes has adverse effects on cardiac function in male and non-pregnant mice and that lactation contributes to the development of postpartum cardiomyopathy in the heart with APJ overexpression. PMID: 27033703 Endothelial CXCR4 is negatively regulated by miR-139-5p, whose transcription is in turn induced by laminar flow and APLN/APLNR signalling. PMID: 27068353 apelin is produced by arterial endothelial cells (ECs) during embryogenesis, induces chemotaxis of venous ECs, and promotes the production of secreted Frizzled-related protein 1 by apelin receptor(+) ECs PMID: 25920569 Findings demonstrate a stimulatory role for the islet cell apelin-APJ signaling axis in regulation of pancreatic islet homeostasis and in metabolic induced beta-cell hyperplasia. PMID: 25965959 ERG and APLNR are essential for endothelial homeostasis in venules in the lung and that perturbation in ERG-APLNR signaling is crucial for the development of pulmonary veno-occlusive disease. PMID: 25062690 These findings suggest that apelin-APJ signaling is a potential therapeutic target in the treatment of vasculogenic erectile dysfunction. PMID: 23578329 regulates the Nodal/Bone Morphogenetic Protein antagonist Cerberus and the Baf60c/Smarcd3 subunit of the Brg1/Brm-associated factors (BAF) chromatin-remodelling complex PMID: 23787002 In obese and insulin-resistant mice, plasma apelin concentration after fasting was not modified but, the gene-expression level of the APL/APJ system was augmented in the white adipose tissue and reduced in the brown adipose tissue, liver and in kidneys. PMID: 23747606 These findings imply that the pancreatic apelin-APJ system functions to curb the inflammatory and fibrosis responses during pancreatitis, and that apelin reduces inflammation and fibrosis by reducing neutrophil recruitment and PSC activity. PMID: 23681476 More than half of the expected Apj-/- embryos died in utero because of cardiovascular developmental defects. Apelin-APJ signaling plays a novel role as a potent regulator of endothelial MEF2 function in the developing cardiovascular system. PMID: 23603510 Apelin-APJ signalling may promote Fas-induced liver injury at least partially via JNK activation. PMID: 23121371 Centrally administered apelin-13 elicited depression-like behavior in mice, which was mediated via APJ receptor and kappa-opioid receptor, but not CRF receptor. PMID: 22728209 We conclude that apelin functions as a new and potent chemoattractant for circulating cKit+/Flk1+/Aplnr+ cells during early myocardial repair, providing myocardial protection against ischemic damage by improving neovascularization via paracine action. PMID: 22753078 study found activation of ATreceptors stimulates apelin secretion in Ca(2), protein kinase C and MAPK kinase dependent ways; activation of AT receptors inhibits apelin secretion through cAMP and cGMP dependent pathways; expression of apelin receptor is si PMID: 22249006 data indicate that APJ is a bifunctional receptor for both mechanical stretch and the endogenous peptide apelin; by sensing the balance between these stimuli, APJ occupies a pivotal point linking sustained overload to cardiomyocyte hypertrophy PMID: 22810587 the novel peptide apelin and its receptor APJ can induce the morphological and functional maturation of blood vessels in tumors PMID: 22037214 Apelin receptor mRNA and apelin-13 binding site distribution in mouse tissues PMID: 22197493 endothelial cells promote the maturation of astrocytes through the apelin/APJ system in mice PMID: 22357924 Disruption of apelin-APJ signaling can exacerbate pulmonary hypertension mediated by decreased activation of AMP-activated kinase and eNOS. PMID: 21233449 Apelin receptor expression by smooth muscle cells provides a paracrine pathway in injured vessels that allows endothelial-derived apelin to stimulate their division and migration into the neointima. PMID: 20176814 Role for the apelinergic system in mechanisms controlling fluid homeostasis, particularly at a neuroendocrine level. PMID: 20136689 data support a role for the apelin-APJ system in the regulation of smooth muscle, epithelial and goblet cell function in the GI tract PMID: 19660504 Expression of the murine msr/apj receptor and its ligand apelin is upregulated during formation of the retinal vessels. PMID: 11744380 APJ exerts the hypotensive effect in vivo and plays a counterregulatory role against the pressor action of angiotensin II PMID: 15087458 Data show that the apj receptor is expressed in pancreatic islets and that apelin-36 inhibits glucose-stimulated insulin secretion both in vivo and in vitro. PMID: 15970338 APJ/apelin-meidated molecular mechanisms for cell migration were reported. PMID: 16211245 APJ is unlikely to be a gene causing idiopathic dilated cardiomyopathy, but the independent correlation between the 212A allele and a better prognosis suggests that it might act as a modifier gene. PMID: 17826642 The apelin-APJ system is a mediator of oxidative stress in vascular tissue, and thus we propose it to be a critical factor in atherogenesis under high-cholesterol dietary conditions. PMID: 17884970 Involved in the regulation of blood vessel diameter during angiogenesis. PMID: 18200044 apelin/APJ signaling pathways play a critical role in the development of the functional vascular network in adipose tissue. PMID: 18708591 physiological role for APJ in mechanisms of water intake and fluid retention suggests an anti-diuretic effect of apelin in vivo PMID: 19578099 Results demonstrate that endogenous apelin-APJ signaling plays a modest role in maintaining basal cardiac function in adult mice with a more substantive role during conditions of stress. PMID: 19767528

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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.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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