Cellular and Molecular Biology

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human ATXN2. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human ATXN2. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human ATXN2, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human ATXN2 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse GDF10. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse GDF10. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse GDF10, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse GDF10 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Rat MuRF1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Rat MuRF1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Rat MuRF1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Rat MuRF1 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse OVA sIgG1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse OVA sIgG1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse OVA sIgG1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse OVA sIgG1 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human TRIM72. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human TRIM72. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human TRIM72, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human TRIM72 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Rat OXR1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Rat OXR1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Rat OXR1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Rat OXR1 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human IFI16. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human IFI16. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human IFI16, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human IFI16 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human SIGLEC14. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human SIGLEC14. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human SIGLEC14, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human SIGLEC14 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Mouse pMAPT/pTAU. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Mouse pMAPT/pTAU. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Mouse pMAPT/pTAU, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Mouse pMAPT/pTAU in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human MPC2. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human MPC2. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human MPC2, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human MPC2 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Rat PAP. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Rat PAP. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Rat PAP, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Rat PAP in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human PAP. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human PAP. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human PAP, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human PAP in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human TrkA/NTRK1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human TrkA/NTRK1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human TrkA/NTRK1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human TrkA/NTRK1 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Human MuRF1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Human MuRF1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Human MuRF1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Human MuRF1 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Rat GDF10. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Rat GDF10. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Rat GDF10, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Rat GDF10 in the samples is then determined by comparing the OD of the samples to the standard curve.</p>

<p>Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive, and cause the gradual weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore, dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.Treatments of dystrophin disorders are in clinical trial including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (2690-2700), has been tested via western blot, mass spectrometry, immunostaining and RT-PCR to try and provide the most robust method of validation of dystrophin levels possible. Further study with this dystrophin fragment could prove to be a vital step in the understanding and treatment of dystrophin disorders. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.</p>

<p>1D,6L-Lanthionine vasopressin</p>

<p>LP2</p>

<p>Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive, and cause the gradual weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore, dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.Treatments of dystrophin disorders are in clinical trial including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (2690-2700), has been tested via mass spectrometry to provide a more reliable method of validation of dystrophin levels. Further study with this dystrophin fragment could prove to be a vital step in the understanding and treatment of dystrophin disorders. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.</p>

<p>Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive, and cause the gradual weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore, dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.Treatments of dystrophin disorders are in clinical trials including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (50-61), has been used to try and create a quantifiable method that is reproducible. The method used was not successful, but dystrophin (50-61) remains a useful tool to create a potential quantification method for diagnosis and progress of dystrophin disorders as it was effectively detected by mass spectrometry and Western blot. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.</p>

<p>EHD1 is a member of the C-terminal EPS15-Homology Domain-containing (EHD) protein family and is involved in recycling cell surface receptors.</p>

<p>The Dystrophin protein, encoded by the dystrophin gene, is part of the dystrophin glycoprotein complex which connects the inner cytoskeleton to the extracellular matrix in muscle fibres. This allows the muscle cell plasma membrane to remain structurally stable.Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive and cause the gradually weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.</p>

<p>Forms of inherited muscular dystrophy such as Duchenne muscular dystrophy (DMD) and Becker muscular dystrophy (BMD) result from mutations targeting the dystrophin gene. These disorders are X-linked, progressive, and cause the gradual weakening of the muscles leading to respiratory failure and ultimately reduces the patient lifespan.In DMD, mutations lead to the production of premature stop codons and hence the truncated dystrophin protein product is vulnerable to nonsense mediated decay and degradation. Therefore, dystrophin production in muscle cells is reduced. On the other hand, nonsense mutations which also contribute to DMD, cause exon skipping in BMD and result in an internally truncated protein product which are partially functional. The symptoms of BMD are later onset compared with DMD which develop in patients between 2 to 7 years.Treatments of dystrophin disorders are in clinical trials including antisense oligonucleotide exon skipping and gene therapy. However, the efficacies of these treatments are not easily quantified. Currently levels of muscular dystrophin are quantified by western blot which can be unreliable. The peptide provided here, aligning residues dystrophin (396-405), has been shown to provide absolute quantification of dystrophin levels from biopsies using parallel reaction monitoring. This will hopefully allow better management of dystrophin disorders with better quantifications tools based on dystrophin (396-405). Further study with this dystrophin fragment could prove to be a vital step in the understanding and treatment of dystrophin disorders. Within our catalogue we also have other peptides tested for dystrophin quantification available plus the full-length dystrophin protein.</p>