| Description | ESRP1 Human Pre-designed siRNA Set A contains three designed siRNAs for ESRP1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ESRP1 siRNA-1: 5 nmol (HPLC) ESRP1 siRNA-2: 5 nmol (HPLC) ESRP1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control:ESRP1 Human Pre-designed siRNA Set A contains three designed siRNAs for ESRP1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ESRP1 siRNA-1: 5 nmol (HPLC) ESRP1 siRNA-2: 5 nmol (HPLC) ESRP1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... Read More | Sequence:Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-AlaBiochemical mechanism:Amyloid protein β Protein segment 1-42 (A β 1-42) It has antioxidant and neuroprotective Sequence:Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Ile-AlaBiochemical mechanism:Amyloid protein β Protein segment 1-42 (A β 1-42) It has antioxidant and neuroprotective properties. Amyloid protein β Protein accumulation is associated with Alzheimer's disease (AD) and Down syndrome. A β 1-42 regulates cholesterol transport and acts as a transcription factor. It may also have anti-inflammatory and antimicrobial effects.Application:Amyloid protein is found in the brain of patients with Alzheimer's disease and Down syndrome β- The main segment of the protein.Amyloid protein β Protein fragments 1-42 have been used to:1. A β Preparation of 1-42 oligomer2. Western blot analysis3. Immunomagnetic Reduction (IMR) Plasma A β 42 Detected interference test4. Study the effect of resveratrol on A β 1-42 induced impairment of spatial learning, memory and synaptic plasticity5. Study A β Role in epithelial cell culture... Read More | Inquire | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.ApplicationUseful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research... Read More | Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by Background:VCAM-1, also known as CD106, is an immunoglobulin (Ig)-like adhesion molecule that is mainly expressed in endothelial cells and other cell types including macrophages, dendritic cells, neurons, smooth muscle cells, fibroblasts, and oocytes. It plays a critical role in inflammation by recruiting leukocytes to acute and chronic inflammation sites. Alternatively-spliced forms are known to occur, but the most common form is a type I transmembrane protein with a 674 aa extracellular domain (ECD) that includes seven C2-type immunoglobulin domains, a 22 aa transmembrane segment, and a 19 amino acid (aa) cytoplasmic tail. Within the ECD, human VCAM-1 shares 75% and 76% aa sequence identity with the mouse and rat VCAM-1, respectively. VCAM-1 binds to leukocyte integrins alpha 4 beta 1 (VLA-4) and alpha 4 beta 7. During the inflammatory adhesion mechanism, activated integrins halt rolling leukocytes and attach them firmly to the vascular endothelium. The VCAM-1:VLA-4/ alpha 4 beta 7 interaction is also thought to be involved in the extravasation of white blood cells through the blood vessel wall to sites of inflammation. ELISA techniques have shown that detectable levels of soluble VCAM-1 are present in the biological fluids of apparently normal individuals, but elevated levels of serum VCAM-1 are indicative of future Atrial Fibrillation incident as well as liver disease. Tumor cells use overexpression of VCAM-1 as means of escaping immune surveillance.Post-translational modifications：Sialoglycoprotein.Function:Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with the beta-1 integrin VLA4 on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/VLA4 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation... Read More |