Recombinant Rat Insulin-1 (INS1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-08988P
Greater than 85% as determined by SDS-PAGE.
Greater than 85% as determined by SDS-PAGE.

Recombinant Rat Insulin-1 (INS1) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-08988P
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Product Overview

Description Recombinant Rat Insulin-1 (INS1) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 85% as determined by SDS-PAGE.
Uniprotkb P01322
Target Symbol INS1
Synonyms Ins1; Ins-1; Insulin-1 [Cleaved into: Insulin-1 B chain; Insulin-1 A chain]
Species Rattus norvegicus (Rat)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence FVKQHLCGPHLVEALYLVCGERGFFYTPKS
Expression Range 25-54aa
Protein Length Partial
Mol. Weight 19.4 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 Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular Location Secreted.
Protein Families Insulin family
Database References

Gene Functions References

  1. In conclusion, TRPV4 differently regulates insulin mRNA expression in INS-1E cells via ERK1/2 and NO-dependent mechanisms. PMID: 28359774
  2. CART is important for maintaining the beta-cell phenotype. PMID: 28237718
  3. Expression of ghrelin and ghrelin receptor and glucose stimulated insulin secretion (GSIS) of pancreatic islets. PMID: 28410130
  4. glucagon plus insulin increases FGF21 transcription by stimulating ATF4 expression PMID: 28188284
  5. Under insulin stimulation, and in spite of the less activated mTOR function in high altitude rats, low altitude rats had higher glycogen content and reduced levels of gluconeogenic enzymes with a more enhanced insulin signaling, mainly due to higher levels of phosphorylated IRS1. PMID: 28084108
  6. Reduced sortilin levels associate with lower VLDL apo B secretion. Sortilin facilitates VLDL-B100 secretion by insulin sensitive McArdle RH7777 cells. PMID: 27495870
  7. Data show that quercetin acutely stimulates insulin release, inhibits cell proliferation and induces apoptosis of INS-1 beta cells. PMID: 27336168
  8. Insulin deficiency increases the expression of IGF-1 and IGF-1R in renal mesangial cells and the kidney of diabetic rats, which contributes to the development of diabetic nephropathy. PMID: 26775660
  9. Data suggest that rosuvastatin has the potential to increase basal insulin secretion and reduce glucose-induced insulin secretion. PMID: 26986474
  10. These results identify a novel role for Jagn1 in regulating proinsulin biosynthesis. PMID: 26882284
  11. Data suggest glucose-induced insulin secretion is first up-regulated (acute infection), then down-regulated (chronic infection) in beta cells infected with S. aureus; Pla2g4a is up-regulated in acute infection; Pla2g6 is up-regulated in chronic infection. PMID: 26632509
  12. These observations support the hypothesis that glucagon acts via adenylate cyclase to decrease hepatic GSH levels and induce insulin resistance. PMID: 25961284
  13. Gamma conglutin and glibenclamide increased Ins-1 gene expression in diabetic rats. PMID: 24894193
  14. Data suggest neural mechanism of allostatic insulin secretion in male rats fed liquid diet as meals; allostasis leads to postprandial insulin secretion by pancreatic islets suggestive of neural/neurosecretory regulation to prevent hyperglycemia. PMID: 25159330
  15. Maximal upregulation of many unfolded protein response genes in response to mutant proinsulin production required IRE1. PMID: 25011481
  16. Data indicate that, gestational Di-(2-ethylhexyl)phthalate (DEHP) exposure predisposes F1 offspring to glucometabolic dysfunction by down-regulating the expression of critical genes involved in the insulin signalling pathway. PMID: 25232145
  17. analysis of organization of the beta-structure of rat insulin reveals key regions essential for the propagation and cytotoxicity of amyloid fibrils PMID: 24569992
  18. Data suggest that responsiveness of pancreatic beta cells to glucose level resulting in secretion of insulin involves Glp1/Glp1r (glucagon-like peptide-1/glucagon-like peptide-1 receptor) signaling and GLP1/Glp1r agonists act as hypoglycemic agents. PMID: 24425760
  19. Data indicate that miR-183 was decreased and Foxo1 was upregulated during conversion of dental pulp cells (DPCs) to insulin-producing cells. PMID: 24440707
  20. miR-25 and miR-92a are found as direct modulators of insulin expression; overexpression of miR-25 or miR-92a reduced insulin expression;inhibition of miR-25 and miR-92a expression promoted insulin expression and ultimately enhanced glucose-induced insulin secretion PMID: 24084692
  21. B-cell translocation gene 2 (BTG2) is a crucial regulator in GLP-1-induced insulin gene expression and insulin secretion via upregulation of pancreatic duodenal homeobox-1 (PDX-1) in pancreatic beta-cells. PMID: 23703573
  22. investigation of role of microtubules/actin cytoskeleton in insulin-stimulated glucose uptake in skeletal muscle: Data suggest sequence of reorganization of microtubules, actin remodeling, translocation of GLUT4, and glucose uptake. PMID: 22996137
  23. Exogenous and endogenous ghrelin counteracts GLP-1 action to stimulate cAMP signaling and insulin secretion in islet beta-cells PMID: 22750144
  24. adiponectin in the serum from CR animals increases NO* signaling by activating the insulin pathway PMID: 22319612
  25. Insulin entry into muscle involves a saturable process in the vascular endothelium PMID: 22002008
  26. results revealed a novel function for brain insulin in CTA and an additional source of local synthesis, the central and/or basolateral nuclei of the amygdala. PMID: 22119580
  27. Per-Arnt-Sim (PAS) domain-containing protein kinase (PASK) has a role in insulin hypersecretion PMID: 22065581
  28. Estrogen-related receptor gamma (ERRgamma) is a novel transcriptional regulator of phosphatidic acid phosphatase, LIPIN1, and inhibits hepatic insulin signaling PMID: 21911493
  29. NAD(P)H oxidase is an important source of superoxide in pancreatic islets and the activity of NAD(P)H oxidase is involved in the control of insulin secretion by palmitate. PMID: 20857410
  30. Insulin increased plasma membrane GLUT4 and GLUT1 content 30 and 40 min after treatment and CD36 content in plasma membrane fraction. PMID: 21773965
  31. Insulin (Ins) release is altered by anesthetics. PMID: 18165568
  32. insulin stimulates cell proliferation and c-Myc expression in colon cancer cell lines HT29 and Caco-2, intestinal non-cancer cell line IEC-6, and primary fetal rat intestinal cell (FRIC) cultures. PMID: 17993259
  33. the stimulation of glucose uptake in response to insulin or metabolic stress is dependent in cardiomyocytes on the presence of intact microtubules. PMID: 18063688
  34. Insulin down-regulates specific activity of ATP-binding cassette transporter A1 for high density lipoprotein biogenesis through its specific phosphorylation PMID: 21402379
  35. C-peptide may contribute to plaque development and restenosis formation in patients with insulin resistance and early type 2 diabetes mellitus. (C-peptide) PMID: 17068290
  36. AS160 phosphotyrosine-binding domain constructs inhibit insulin-stimulated GLUT4 vesicle fusion with the plasma membrane PMID: 21454690
  37. Data support the hypothesis that brain insulin is required to support optimal baroreflex function and that a decrease in brain insulin contributes to the fall in baroreflex gain during pregnancy. PMID: 21149828
  38. beta2-Syntrophin is a Cdk5 substrate that restrains the motility of insulin secretory granules. PMID: 20886068
  39. Intrauterine growth retardation leads to the functional change of insulin secretion in the newborn. PMID: 20225168
  40. This study identified second messenger systems in neuropeptide Y neurons of arcuate nucleus which regulate neuron activity and physiological processes such as the control of food intake and body weight, under the combined control of insulin and leptin. PMID: 19671839
  41. Leptin and insulin induce mutual resistance for nitric oxide synthase III activation in adipocytes PMID: 19728324
  42. induction of c-myc expression suppresses gene transcription PMID: 11799123
  43. Insulin preincubation effects on rat vessel contractile responses: role of the endothelium cycooxygenase and nitric oxide synthase pathways. PMID: 11824479
  44. mechanisms involved in the insulin-induced acceleration of ET1 contractions; role of the sarcoplasmic reticulum and calcium. PMID: 11824480
  45. pancreatic release of insulin inhibited by ghrelin PMID: 11834435
  46. effects of insulin and the degree of muscle loading on the phosphorylation of Ser(2448), a site in the mammalian target of rapamycin (mTOR) phosphorylated by protein kinase B (PKB) in vitro PMID: 11884412
  47. Glucagon-like peptide-1 analogue LY315902: effect on intestinal motility and release of insulin and somatostatin PMID: 12047915
  48. endogenously released insulin plays an important role in potentiating pancreatic secretion stimulated by exogenous cholecystokinin (CCK) and intraduodenal infusion of casein PMID: 12120208
  49. the signalling pathways and the effects of insulin were compared to those of glutamine and leucine in isolated hepatocytes from normal and streptozotocin-diabetic rats PMID: 12153571
  50. Insulin modulates GLUT4 trafficking at multiple steps, including not only the endocytotic and exocytotic rates, but also the two rate coefficients coupling the three intracellular compartments. PMID: 12450403

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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