Recombinant Mouse Peptide Yy (PYY) Protein (GST)

Name: Recombinant Mouse Peptide Yy (PYY) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-00696P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Peptide Yy (PYY) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9EPS2
Target Symbol	PYY
Synonyms	(PYY)(Peptide tyrosine tyrosine)(3-36)(PYY-II)
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	YPAKPEAPGEDASPEELSRYYASLRHYLNLVTRQRY
Expression Range	29-64aa
Protein Length	Partial
Mol. Weight	31.2 kDa
Research Area	Others
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	This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility.
Subcellular Location	Secreted.
Protein Families	NPY family
Database References	KEGG: mmu:217212 STRING: 10090.ENSMUSP00000017455 UniGene: PMID: 29455414 These results indicate that endogenous PYY has a hypoalgesic effect on somatic thermal and visceral chemical pain. The effect on visceral pain seems to be mediated by peripheral Y2 receptors. PMID: 28106168 Study suggests that PYY3-36 mediated signalling via Y5 receptors may counteract the anorectic effects that it mediates via the Y2 receptor, consequently lowering bodyweight in the absence of Y5 signalling. PMID: 28485050 expression of PYY and its NPY receptors on mouse islets and immortalised rodent and human beta-cells was examined. PMID: 27465830 Angiotensin II stimulates PYY secretion, in turn inhibiting epithelial anion fluxes, thereby reducing net fluid secretion into the colonic lumen. PMID: 27447725 new information on the cell specific localization of NUCB2/nesfatin-1 in the intestinal mucosa, and a novel function for nesfatin-1 in modulating intestinal CCK and PYY expression and secretion PMID: 26920055 Data (including data from studies in transgenic mice) suggest neurotensin (Nts), glucagon-like peptide I (GLP-1), and peptide YY (Pyy) are closely co-expressed and co-secreted within enteroendocrine cells in ileum mucosa. PMID: 26469136 pancreatic islet-derived PYY plays an important role in controlling glucose homeostasis through the modulation of beta-cell mass and function PMID: 26125465 The patterns of colocalisation of the K cell marker, glucagon-like insulinotropic peptide, and the L cell markers, glucagon like peptide-1 and peptide YY, in enteroendocrine cells of the small intestine and colon of mouse and pig, were investigated. PMID: 25378285 Glutamine stimulates the co-release of endogenous GLP-1 and PYY from mucosal L-cells resulting in paracrine GLP-1 and Y1 receptor-mediated electrogenic epithelial responses. PMID: 23992397 Data suggest that an intestinal enteroendocrine cell line (STC-1) secrets PYY constitutively releasing PYY into cell culture media; linoleic acid and conjugated linoleic acid 9,11 are potent PYY secretagogues; most short-chain fatty acids are not. PMID: 22926626 Suggest that PYY might be one critical mediator of deoxynivalenol-induced anorexia and, ultimately, growth suppression. PMID: 22903826 gut peptide PYY is critical for the control of bone remodeling. PMID: 22792209 a lineage of mature enteroendocrine cells have the ability to coexpress members of a group of functionally related peptides: CCK, secretin, GIP, GLP-1, PYY, and neurotensin PMID: 23064014 PYY reduces food intake while enhancing lipogenic capacity and insulin action, likely contributing to fuel assimilation in the postprandial state. PMID: 22575886 Data suggest that Pyy expression in hindbrain is regulated by nutritional factors and correlates with circulating PYY and leptin; Pyy decreases in acute starvation, prolonged caloric restriction, and after bariatric surgery (enterogastroanastomosis). PMID: 22761162 PYY appears to regulate beta cell function and survival via the receptor Y(1/2). PMID: 22562022 This study demonistrated that PYY has an important role in the regulation of olfactory neuron differentiation. PMID: 22354615 dietary resistant starch is well tolerated, fermented in the colon, and stimulates colonic expression of proglucagon and PYY mRNA, and adiponectin protein in visceral fat. PMID: 22174009 PYY(3-36) is also present in murine as well as in human saliva PMID: 22028819 Gene expressions of ghrelin, PYY, and CCK was increased in the gastrointestinal tract of the hyperphagic intrauterine growth restriction rat offspring. PMID: 21264794 PYY/PYY(3-36) potently inhibits basal and stress/serotonin/cholinergic-stimulated propulsive colonic motor function in conscious mice, likely via Y(2) receptors PMID: 19892938 Langerhans cells and a certain BALB/c and A/J mice epidermis-derived dendritic cell line contain mRNA for peptide yy PMID: 12372697 targeted disruption of the peptide YY gene does not perturb terminal endocrine cell differentiation or the control of food intake and energy homeostasis PMID: 15870288 Data show that the sustained inhibition of gastric secretion due to tumours producing PYY/enteroglucagon in transgenic mice is associated with an increase in AQP4 expression and a down-regulation of H(+)/K(+)-ATPase in parietal cells. PMID: 15898955 Reduced expression in gastrin-cholecystokinin knockout mice. PMID: 16002530 reduced PYY levels may predispose to the development of obesity, particularly with ageing or under conditions of high-fat feeding, as demonstrated in peptie YY-deficient mice. PMID: 16680491 We generated Pyy null mice, which were selectively resistant to the satiating and weight-reducing effects of protein and developed marked obesity that was reversed by exogenous PYY treatment. PMID: 16950139 that PYY may be a mediator of islet cell development, as well as a cofactor for growth factor responses, not only during fetal pancreas formation but also during regeneration in adult mice. PMID: 17185798 Overexpression of PYY by transgenic technique, chronic administration of PYY into normal pregnant mice, or deletion of the PYY Y1 receptor produced neural tube defects. PMID: 17400914 Diet-induced obese mice had low plasma PYY, which may have caused compensatory up-regulation of PYY and Y2 receptor densities in medulla. PMID: 17615145 Endogenous PYY plays a critical role in regulating bone mass. In comparison, its role in regulating body weight is minor and is confined to situations of high-fat feeding. PMID: 17920065 Activation of neurons in the nucleus of the solitary tract following administration of T2R agonists to the GI tract involves CCK(1) and Y(2) receptors located on vagal afferent terminals in the gut wall. PMID: 18003792 PYY-immunoreactive (ir) cell bodies were localized exclusively to the gigantocellular reticular nucleus (Gi) of the rostral medulla. The highest density of PYY fibers was present within the solitary tract nucleus. PMID: 18022952 there was no effect of PYY transgenic over expression on basal or fasting-induced food intake PMID: 18164057

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.