| Description | FAKsiRNA-3 is a small interfering RNA that targets FAK messenger RNA | Arachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towardsArachis hypogaea lectin or Peanut Agglutinin (PNA) is isolated from peanuts and purified by affinity chromatography. The lectin has a molecular weight of 110 kDa and consists of four identical subunits of approximately 27 kDa each. PNA is a carbohydrate-free protein that displays specificity towards ?-D-Gal(1-3)-D-galNAc. It has potent anti-T activity and can be used to distinguish between human lymphocyte subsets. PNA has been used in tumour tissue determination for transitional mucosa malignancies. The lectin also agglutinates neuraminidase-treated human erythrocytes at < 0.1 µg/ml after trypsin treatment of cells and its activity is inhibited by lactose and galactose. PNA lectin is provided as a white to light yellow lyophilized powder from a buffer containing 10 mM NH4HCO3. The purity is determined by SDS-PAGE, which generates one band at 25-27 kDa.● Ultrapure quality ● Strong anti-T activity ● Sugar specificity: ?-D-Gal-(1-3)-D-GalNAc ● Agglutinates rabbit erythrocytes at < 0.1 µg/ml after trypsin treatment of the cells ● Lyophilized powderProbe in histochemistry and immuno-histochemistry;Human erythrocyte/lymphocyte studies... Read More | Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Protease-Activated Receptor-1, PAR-1 Agonist is a selective proteinase-activated receptor1 (PAR-1) agonist peptide. Protease-Activated Receptor-1, PAR-1 Agonist corresponds to PAR1 tethered ligand and which can selectively mimic theactions of thrombin via this receptorIn VitroProtease-Activated Receptor-1, PAR-1 Agonist induces activation of protein kinase C isoenzymes alpha and epsilon in human HT-29 colon carcinoma cells expressing PAR1 endogeneously. On the cellular level, Protease-Activated Receptor-1, PAR-1 Agonist and thrombin prompted HT-29 cell migration and matrix adhesion by a PKCepsilon-dependent mechanism as concluded because of the inhibition of PAR1-mediated effects by the PKC inhibitor bisindolylmaleimide I and the PKCepsilon translocation inhibitory peptide EAVSLKPT but not by the PKC inhibitor Gö 6976. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:PAR-1... Read More | Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and Purity> 95% by SDS-PAGE and HPLC analyses.FunctionGrowth factor that controls proliferation and cellular differentiation in the retina and bone formation. Plays a key role in regulating apoptosis during retinal development. Establishes dorsal-ventral positional information in the retina and controls the formation of the retinotectal map (PubMed:23307924). Required for normal formation of bones and joints in the limbs, skull, digits and axial skeleton. Plays a key role in establishing boundaries between skeletal elements during development. Regulation of GDF6 expression seems to be a mechanism for evolving species-specific changes in skeletal strucutres. Seems to positively regulates differentiation of chondrogenic tissue through the growth factor receptors subunits BMPR1A, BMPR1B, BMPR2 and ACVR2A, leading to the activation of SMAD1-SMAD5-SMAD8 complex. The regulation of chondrogenic differentiation is inhibited by NOG (PubMed:26643732). Also involved in the induction of adipogenesis from mesenchymal stem cells. This mechanism acts through the growth factor receptors subunits BMPR1A, BMPR2 and ACVR2A and the activation of SMAD1-SMAD5-SMAD8 complex and MAPK14/p38... Read More | Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. Purity:>98%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Heme oxygenase (HMOX) is the rate limiting enzyme in heme catabolism. It cleaves heme to biliverdin, carbon monoxide, and iron. The biliverdin is subsequently converted to bilirubin by biliverdin reductase. The mechanism of HMOX is unique in that heme serves as the substrate of the enzyme and as the prosthetic group for the activation of iron-bound O2. HMOX activity is highest in spleen where senescent erythrocytes are sequestered and destroyed. Two isoforms, HMOX1 and HMOX2, are expressed in most tissues. HMOX1 is an inducible enzyme in response to heme, heavy metals, oxidative stress, cytokines, and many drugs. Whereas HMOX2 displays a constitutive expression. HMOX1 is expressed mainly in spleen, liver, and kidney, and HMOX2 is prominently expressed in the brain and testes. The increased expression of HMOX1 levels is related to a variety of pathological states, where it functions as a cytoprotective molecule through its by products. HMOX1 also plays important roles in the regulation of cell proliferation, differentiation, and apoptosis... Read More |