Pig Insulin,INS ELISA Kit

Instructions
Code CSB-E06828p
Size 96T,5×96T,10×96T
See More Details 24T ELISA kits trial application
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Product Details

Target Name insulin
Alternative Names INS ELISA Kit; Insulin [Cleaved into: Insulin B chain; Insulin A chain] ELISA Kit
Abbreviation INS
Uniprot No. P01315
Species Sus scrofa (Pig)
Sample Types serum, plasma, tissue homogenates
Detection Range 2 μIU/mL-400 μIU/mL
Sensitivity 1 μIU/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Metabolism
Assay Principle quantitative
Measurement Competitive
Precision
Intra-assay Precision (Precision within an assay): CV%<15%      
Three samples of known concentration were tested twenty times on one plate to assess.  
Inter-assay Precision (Precision between assays): CV%<15%      
Three samples of known concentration were tested in twenty assays to assess.    
             
Linearity
To assess the linearity of the assay, samples were spiked with high concentrations of pig INS in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
  Sample Serum(n=4)  
1:1 Average % 96  
Range % 84-105  
1:2 Average % 93  
Range % 89-99  
1:4 Average % 95  
Range % 89-101  
1:8 Average % 95  
Range % 83-103  
Recovery
The recovery of pig INS spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample Type Average % Recovery Range  
Serum (n=5) 96 91-101  
EDTA plasma (n=4) 98 92-104  
             
             
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
μIU/ml OD1 OD2 Average    
0 1.800 1.864 1.832    
2 1.569 1.581 1.575    
8 1.304 1.327 1.316    
32 0.812 0.805 0.809    
100 0.389 0.393 0.391    
400 0.180 0.183 0.182    
Troubleshooting
and FAQs
ELISA kit FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 3-5 working days

Target Data

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.
Gene References into Functions
  1. We expect that these insulin-deficient pigs can be used in diabetes research to test the efficacy and safety of new drugs and the recipient of islet transplantation to investigate optimal transplantation strategies. PMID: 29691708
  2. Study used well-tempered bias exchange metadynamics simulations to determine the equilibrium ensembles of an insulin molecule under amyloidogenic conditions of low pH and high temperature. The folded state of a single insulin molecule was shown to be the most stable, longest-lived state even under amyloidogenic conditions. PMID: 28445749
  3. The findings are consistent with previous studies that indicate a link between Na,K-ATPase activity and SFK signaling. PMID: 27748508
  4. PTPLAD1 and AMPK are rapidly compartmentalized within the plasma membrane (PM) and Golgi/endosome fractions after insulin stimulation and that ATIC later accumulates in the Golgi/endosome fraction. PMID: 25687571
  5. Pdx-1, MafA and NeuroD1 bind to the A, C and E elements in the insulin promoter and regulate the transcriptional activity of the insulin promoter. PMID: 24825179
  6. The interplay of the adiponectin system, TNFalpha and insulin at a transcriptional level and, their effects on the adipogenic transcription factor PPARgamma, as well as on the activation of main insulin signaling pathways, is reported. PMID: 24846393
  7. Thermodynamics of insulin unfolding have been quantified by differential scanning calorimetry and thermal unfolding measurements to determine the extent and nature of their stabilization of the insulin hexamer. PMID: 24811232
  8. Exposing the hydrophobic core of insulin can induce the increase of amyloidogenicity and formation of higher-order polymerized fibrils, which is less toxic to membranes. PMID: 24041697
  9. Data suggest that a mutation in INS (C94Y) results a transgenic disease model for the investigation of permanent neonatal diabetes. PMID: 23274907
  10. The results show that modulation of plasma insulin levels by dietary carbohydrates seems possible in anabolic sows, but IGF-I levels are less easily modified. PMID: 21635573
  11. insulin increased GCLc promoter activity, which required a prerequisite increase or decrease in medium glucose PMID: 21871559
  12. SOCS3 is an important negative regulator of insulin signaling in porcine adipocytes. PMID: 20683642
  13. Plasma concentrations of insulin in pigs fed once per day were lower before feeding than after the meal. Plasma concentrations of insulin in ad libitum fed pigs exhibited random fluctuations. PMID: 20399063
  14. Data show that an expression cassette containing 1500bp of the porcine insulin promoter 5' UTR confers robust and specific transgene expression to beta-cells in vitro and in transgenic mice. PMID: 19682540
  15. Neutron diffraction data for T(6) porcine insulin were collected to 2.1 A resolution from a single crystal partly deuterated by exchange of mother liquor. PMID: 19770501
  16. computational analysis of the altered ionization of the B13 Glu in insulin B9 and B10 mutants of 4INS PMID: 15326283
  17. Results describe the in vitro folding/unfolding of insulin/single-chain insulin. PMID: 16800793
  18. A two-stage in vitro folding pathway of insulin is proposed, with six major folding intermediates captured during the folding process. PMID: 17914645
  19. Streptozotocin is able to impair in vitro neonatal pancreatic beta cell insulin release whereas human cytokines is not. PMID: 17991146
  20. A16Leu had much more significant effects on the foldability of insulin than B17Leu. PMID: 18071885
  21. These data demonstrated that feed allowance level has important consequence on embryo survival, embryo development and uterine development, possibly mediated by changes in concentrations of reproductive hormones. PMID: 18700853
  22. Functional surfaces of insulin were probed by photocross-linking of an extensive set of azido derivatives constructed by chemical synthesis. PMID: 19321435

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Subcellular Location Secreted
Protein Families Insulin family
Database Links

KEGG: ssc:397415

STRING: 9823.ENSSSCP00000025428

UniGene: Ssc.583

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