Recombinant Human Gastric Inhibitory Polypeptide (GIP) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06245P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Human Gastric Inhibitory Polypeptide (GIP) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-06245P
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Product Overview

Description Recombinant Human Gastric Inhibitory Polypeptide (GIP) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 85% as determined by SDS-PAGE.
Activity Not tested.
Uniprotkb P09681
Target Symbol GIP
Synonyms GIP;Glucose-dependent insulinotropic polypeptide;Incretin hormone
Species Homo sapiens (Human)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence YAEGTFISDYSIAMDKIHQQDFVNWLLAQKGKKNDWKHNITQ
Expression Range 52-93aa
Protein Length Full Length of Mature Protein
Mol. Weight 10.0 kDa
Research Area Signal Transduction
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 Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion.
Subcellular Location Secreted.
Protein Families Glucagon family
Database References

HGNC: 4270

OMIM: 137240

KEGG: hsa:2695

STRING: 9606.ENSP00000350005

UniGene: PMID: 29765988

  • The ability of a truncated form of GIP, GIP(3-30)NH2, to antagonize the physiological actions of GIP in glucose metabolism, subcutaneous abdominal adipose tissue blood flow, and lipid metabolism in humans. PMID: 28667118
  • GIP and PP plasma concentrations are lower in pancreatic cancer irrespective of the degree of glucose intolerance as compared to Type 2 diabetic patients and healthy controls. PMID: 28027898
  • Evening postprandial insulin and GIP responses and insulin resistance declined by over 30% after three meals that limited daily carbohydrate intake to 30% compared to no such changes after three 60%-carbohydrate meals, an effect that was independent of pre-meal exercise. PMID: 27798656
  • the stimulatory effect of IGF-1 on GIP promoter support the hypothesis of a functional growth hormone-igf-1-GIP axis PMID: 28179449
  • decreased maternal 25OHD may be associated with decreased cord 25OHD and increased cord GLP-1 and GIP levels, which may be involved with the transfer of maternal glucose to the fetus PMID: 26650343
  • Excess androgen activity might be a factor contributing to alter secretion of incretins in lean polycystic ovary syndrome (PCOS) women. However it could not be ruled out that it is also possible that increased GIP levels might induce hyperandrogenemia in PCOS. PMID: 26895276
  • Our results might indicate an altered DPP4-incretin system and altered immunoregulation including a potentially dysfunctional GLP1(9)(-)(36) signaling in T1DM. PMID: 26434625
  • Fasting GIP concentrations are higher in individuals with a history of cardiovascular disease (myocardial infarction, stroke) when compared with control subjects. PMID: 26395740
  • Data suggest that high levels of blood glucose or AGEs (advanced glycation end products), as seen in hyperglycemia, reduce secretion of insulin by pancreatic beta cells via antagonism of GIP (gastric inhibitory polypeptide)/GIP receptor signaling. PMID: 26221611
  • Data confirm that postprandial plasma levels of glucose-dependent insulinotropic polypeptide (GIP) and insulin (INS) are responsive to glycemic index of foods consumed; glycemic index of breakfast cereals regulate plasma postprandial GIP and INS. PMID: 25852025
  • irisin and GIP might contribute to the development of polycystic ovary syndrome and may also represent novel polycystic ovary syndrome biomarkers PMID: 25029417
  • Data suggest that postprandial blood levels of both GIP and insulin can be regulated by diet; here, inclusion of nopal/Opuntia/cactus (a functional food in traditional Mexican medicine) in breakfast reduces postprandial levels of GIP and insulin. PMID: 25132122
  • phosphatidylinositol 3-kinase gamma has a role in insulin secretion induced by glucose-dependent insulinotropic polypeptide PMID: 25288806
  • These novel results support the notion that the GIP-GIPR axis plays a role in the etiology of central obesity in humans PMID: 25324507
  • Data from studies in healthy Japanese men suggest that plasma GIP levels in postprandial period are dose dependently increased by fat content of meals of ordinary size, despite the amount of additional fat being relatively small. PMID: 24507870
  • Patients with idiopathic gastroparesis exhibit abnormal GIP levels. PMID: 23663508
  • Beta cell connectedness is an inherent property of human islets that is likely to influence incretin-potentiated insulin secretion. PMID: 24018562
  • Data suggest that postprandial plasma levels of glucose-dependent insulinotropic peptide (GIP) and glucagon-like peptide-1 (GLP1) are increased after consumption of buckwheat crackers versus rice crackers in healthy and type 2 diabetic subjects. PMID: 23485142
  • GIP induces an inflammatory and prolipolytic response via the PKA -NF-kappaB-IL-1 pathway and impairs insulin sensitivity of glucose uptake in human adipocytes. PMID: 23092914
  • results indicate postprandial GIP secretion in early-phase after test meal in Japanese patients with type 2 diabetes was positively correlated with BMI, but not those with type 1 diabetes PMID: 22301939
  • Hyperinsulinemia subjects with metabolic syndrome showed increased GIP secretion that could be responsible for the delayed glucagon suppression. PMID: 22391044
  • Data suggest that reduced insulinotropic effect of GIP or GLP-1 (as in type 2 diabetes) can be induced in healthy subjects; this indicates that reduced incretin stimulation of insulin secretion results from insulin resistance/glucose intolerance. PMID: 22319034
  • GIP reduces free fatty acid release from adipose tissue by inhibition of lipolysis or by increased reesterification. PMID: 22179810
  • may have a pro-obesogenic action [review] PMID: 21815989
  • Studies identified some potentially important additional C-terminal interactions of GIP with its N-terminal extracellular receptor domain. PMID: 21539943
  • We report that the human GIP locus was differentially selected in East Asians about 8100 years ago based on the analysis of a nonsynonymous SNP (rs2291725). PMID: 20978139
  • GLP-2, but not GIP, was found to stimulate the release of glucagon in patients with T1DM, suggesting a role for GLP-2 in the postprandial hyperglucagonaemia characterising individuals with T1DM PMID: 20580750
  • These results suggest that Tyr/His(1) and Ile/Thr(7) of GIP/GLP-1 peptides confer differential ligand selectivity toward GIPR and GLP1R. PMID: 20799012
  • We demonstrate for the first time that changes in insulin secretion after lifestyle intervention may be mediated via alterations in GIP secretion from intestinal K-cells PMID: 20200305
  • No statistically significant association was observed between any of the single nucleotide polymorphisms of GIP analysed and type 2 diabetes in our population. PMID: 20673334
  • GIP is expressed in and secreted from pancreatic islets and promotes islet glucose competence and also could support islet development and/or survival. PMID: 20138041
  • a binding mode of GIP to GIPR in which the N-terminal moiety of GIP was sited within transmembrane helices (TMH) 2, 3, 5, and 6 with biologically crucial Tyr1 interacting with Gln224 (TMH3), Arg300 (TMH5), and Phe357 (TMH6). PMID: 20061446
  • Substitution of Glu(3) in GIP with proline produces a novel dipeptidylpeptidase IV-resistant GIP antagonist which inhibits GIP-induced cAMP generation and insulin secretion with high sensitivity and specificity in vitro. PMID: 11820780
  • activates the Raf-Mek1/2-ERK1/2 module via a cyclic AMP/cAMP-dependent protein kinase/Rap1-mediated pathway PMID: 12138104
  • Mutation in promoter region of gip receptor gene are unlikely to underlie GIP-dependent Cushing syndrome. PMID: 12530694
  • Elevated plasma GIP levels are correlated with hyperinsulinemia in the impaired glucose-tolerant state, whereas type 2 diabetes is associated with a failure to secrete adequate amounts of GIP. PMID: 15220248
  • bombesin and nutrients additively stimulate GIP release from GIP/Ins cells. PMID: 15383372
  • Results describe the solution structure of GIP(1-30)amide, the major biologically active fragment of glucose-dependent insulinotropic polypeptide. PMID: 15522230
  • GIP augments glucose-stimulated insulin secretion and acts as an endogenous inhibitor of gastric acid secretion--REVIEW PMID: 15533777
  • GIP stimulates insulin secretion by potentiating events underlying membrane depolarization and exerting direct effects on exocytosis. PMID: 15955806
  • The relationship between insulin resistance and the insulin secretion to GIP suggests that beta cell secretory function in response to different stimuli increases adaptively when insulin sensitivity is diminished, as in gestational diabetes. PMID: 16010522
  • GIP is rapidly degraded into inactive metabolites by the enzyme dipeptidyl-peptidase-IV. (review) PMID: 16142014
  • protein kinase B, LKB1, and AMP-activated protein kinase have roles in activation of lipoprotein lipase by glucose-dependent insulinotropic polypeptide in adipocytes PMID: 17244606
  • study identified a splice site mutation of the Glucose-dependent insulinotropic polypeptide (GIP) gene which results in a truncated protein and provides evidence for association of GIP receptor genotype with cardiovascular disease PMID: 17624916
  • physiologic role for GIP in lipid homeostasis and possibly in the pathogenesis of obesity. PMID: 18054552
  • concomitant expression of Pax6 and Pdx1 is important for glucose-dependent insulinotropic polypeptide expression PMID: 18593849
  • GIP secretion is blunted after the biliopancreatic diversion only in diabetic patients, suggesting a role in insulin resistance and diabetes. PMID: 19229515
  • GIP may mediate the attenuated glucose-stimulated insulin response after exercise/diet interventions PMID: 19351807
  • Inhibition of apoptosis by GIP is mediated via a key pathway involving Akt-dependent inhibition of apoptosis signal-regulating kinase 1, which subsequently prevents the pro-apoptotic actions of p38 MAPK and JNK. PMID: 19748889
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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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