Biotinylated Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-01582P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Biotinylated Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (MBP&His-Avi)

Beta LifeScience SKU/CAT #: BLC-01582P
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Product Overview

Description Biotinylated Recombinant Human Gastric Inhibitory Polypeptide Receptor (GIPR) Protein (MBP&His-Avi) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% 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 E.coli
Tag N-MBP&C-6His-Avi
Target Protein Sequence RAETGSKGQTAGELYQRWERYRRECQETLAAAEPPSGLACNGSFDMYVCWDYAAPNATARASCPWYLPWHHHVAAGFVLRQCGSDGQWGLWRDHTQCENPEKNEAFLDQRLILERLQ
Expression Range 22-138aa
Protein Length Partial
Mol. Weight 61.2 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 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

    • FAQs

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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.

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