Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (His&Myc)

Name: Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04974P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Featured immune checkpoint protein molecules, High-quality recombinant proteins, Immune checkpoint proteins

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Product Overview

Description	Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (His&Myc) is produced by our Mammalian cell expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P48546
Target Symbol	GIPR
Synonyms	GIPR; Gastric inhibitory polypeptide receptor; GIP-R; Glucose-dependent insulinotropic polypeptide receptor
Species	Homo sapiens (Human)
Expression System	Mammalian cell
Tag	N-10His&C-Myc
Target Protein Sequence	RAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQ
Expression Range	22-138aa
Protein Length	Partial
Mol. Weight	18.5
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.
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 is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular Location	Cell membrane; Multi-pass membrane protein.
Protein Families	G-protein coupled receptor 2 family
Database References	HGNC: 4271 OMIM: 137241 KEGG: hsa:2696 STRING: 9606.ENSP00000467494 UniGene: PMID: 28744963 Data suggest that GIPR (gastric inhibitory polypeptide receptor) is among the few GPCRs (G-protein-coupled receptors) which signal through G-proteins (GTP-binding protein Gs alpha subunit, here) both at plasma membrane and in endosomes; recombinant proteins expressed in HEK293 cells were used in these studies. PMID: 27641811 GIPR overexpression does not appear to affect acromegalic patients' clinical features PMID: 28179449 Study shows the internalization of GIPR involving clathrin-coated pits, AP-2 and dynamin and its subsequent intracellular trafficking. GIP stimulates a rapid robust internalization of the GIPR, the major part being directed to lysosomes. PMID: 26225752 The common variant rs10423928 in the GIPR gene is associated with increased risk of stroke in patients with type 2 diabetes. PMID: 26395740 Body mass index change for the A/T+A/A in GIPR genotypes was significantly higher than that for the T/T genotype. rs10423928 may predict weight gain in schizophrenia. PMID: 25321336 The potential future role of gastric inhibitory peptide (GIP) receptors as molecular targets in neuroendocrine neoplasms may be dependent on the tumor grade. PMID: 25591947 Results show that GIPR undergoes trafficking between the plasma membrane and intracellular compartments of both GIP-stimulated and unstimulated adipocytes. PMID: 25047836 GIPR is overexpressed in gastric and duodenal neuroendocrine tumors PMID: 24565507 GIPR expression was downregulated in subcutaneous adipose tissue from obese patients and correlated negatively with body mass index, waist circumference, systolic blood pressure, and glucose and triglyceride levels. PMID: 24512489 GIPR promoter was hypomethylated in type 2 diabetic patients as compared to controls. PMID: 24086540 This study demonstrates an association between a functional GIPR polymorphism Glu354Gln (rs1800437) and Bone mineral density and fracture risk. PMID: 24446656 Compared with the current treatment standard SSTR2, GIPR has only somewhat lesser absolute gene expression in tumor tissue but much lesser expression in normal tissue, making it a promising new target for neuroendocrine tumor imaging and therapy. PMID: 24238043 Structural and pharmacological characterization of novel potent and selective monoclonal antibody antagonists of glucose-dependent insulinotropic polypeptide receptor. PMID: 23689510 Functional expression of a GIP receptor mutant lacking N-glycosylation is rescued by co-expressed wild type GLP1 receptor, which suggests formation of a GIP-GLP1 receptor heteromer. PMID: 22412906 Our prospective, observational study indicates that the type 2 diabetes risk by dietary intake of carbohydrate and fat may be dependent on GIPR genotype. PMID: 22399504 Most of the somatostatin receptor-negative neuroendocrine tumors and GLP-1 receptor-negative malignant insulinomas are GIP receptor positive. PMID: 22112810 The T allele of GIPR rs2287019 is associated with greater improvement of glucose homeostasis in individuals who choose a low-fat, high-carbohydrate, and high-fiber diet. PMID: 22237064 a role of the adipocyte GIPr in nutrient-dependent regulation of body weight and lean mass, but it does not support a direct and independent role for the adipocyte or beta-cell GIPr in promoting adipogenesis. PMID: 22027838 Variations of the GIPR sequence are not associated with childhood obesity. PMID: 20516203 Variants at the GIPR locus associated with 2-h glucose level (rs10423928, beta (s.e.m.) = 0.09 (0.01) mmol/l per A allele, P = 2.0 x 10(-15)), were identified. PMID: 20081857 Proximal 5' flanking region is TATA-less and contains a GC-rich region involved in cellular expression. PMID: 12530665 differences in cellular response to gastric inhibitory polypeptide(GIP) mediated by endothelin-1 may be related to differences in activation of GIP receptor splice variants PMID: 12721154 Glucose-stimulated insulin secretion is maintained despite complete absence of both GIP-1 and GIP receptors. Role for incretin receptors as essential downstream targets for glucoregulatory actions of DPP-IV inhibitors. PMID: 15111503 Proximal promoter of GIP-R gene contains a GC-rich region capable of binding to Sp1 and SP3. PMID: 15666829 the promoter region of the GIP-R gene revealed six consensus sequences important in regulating the reporter gene activity and capable of binding to Sp1 and Sp3 transcription factors PMID: 16087722 GIPR adipose tissue gene expression was significantly lower in insulin resistant obese non-diabetic women PMID: 17395281 GIPR overexpression was observed in pediatric and adult adrenocortical tumors PMID: 18971217 Diabetic kidney lesions of GIPRdn transgenic mice: podocyte hypertrophy and thickening of the GBM precede glomerular hypertrophy and glomerulosclerosis. PMID: 19211686 Our data suggest a potential relevance of GIPR variants for obesity. PMID: 19254363 Decreased TCF7L2 protein levels in type 2 diabetes mellitus correlate with downregulation of GLP-1R and GIP-R. PMID: 19386626

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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.