| Description | Antioxidant peptide A TFA is a short peptide, which contains alternative aromatic or sulfur-containing amino acid. The side chains of Antioxidant peptide A are believed to contribute to strong radical scavenging activities of peptides in the cancer cell.Appearance:SolidBiological Activity:Antioxidant peptide A TFA is a short peptide, which contains alternative aromatic or sulfur-containing amino acid. The side chains of Antioxidant peptide A are believed to contribute to strong radical scavenging activities of peptides in the cancer cell.Appearance:SolidBiological Activity:Antioxidant peptide A TFA is a short peptide, which contains alternative aromatic or sulfur-containing amino acid. The side chains of Antioxidant peptide A are believed to contribute to strong radical scavenging activities of peptides in the cancer cell... Read More | IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 IRAK-4 protein kinase inhibitor 2 (compound 1) is a potent inhibitor of interleukin-1 (IL-1) receptor-associated kinase-4 (IRAK-4), with an IC 50 of 4 µM. IRAK-4 protein kinase inhibitor 2 can be used for the research of inflammatory and immune-related conditions or disordersIn VitroIRAK-4 protein kinase inhibitor 2 (compound 1) also inhibits IRAK-1, with an IC 50 of <10 µM. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:SolidIC50& Target:IRAK4 4 µM (IC 50 )... Read More | Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing Purity＞95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More | Purity≥ 98% SDS-PAGE.FunctionInvolved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：p53 is well known for its key role as a tumor suppressor protein. It is 393 amino acids (aa) in length with a predicted molecular weight of 44 kDa. It belongs to the p53 family that also includes p63 and p73. Structurally, p53 is characterized by an N-terminal transactivation domain, central DNA-binding and oligomerization domains, and a C-terminal regulatory domain. It is thought to exist as a homotetramer, and it exhibits approximately 72% and 76% aa identity with its mouse and rat orthologs, respectively. Mutations in the p53 gene are one of the most frequent genomic events accompanying oncogenic transformation. p53 responds to signals such as DNA damage or cell stress primarily through its actions as a transcription factor. Among its gene targets are a range factors that promote DNA repair mechanisms or apoptosis, including cell cycle regulatory proteins and members the Bcl-2 family. Because of its critical role in genomic homeostasis, p53 activities are tightly regulated by a network of protein-protein interactions, microRNAs, and a range of post-translational modifications, including phosphorylation, acetylation, methylation, and ubiquitination. A widely studied regulator is Murine Double Minute 2 (MDM2). MDM2 is known to suppress p53 activity through direct binding or through its actions as a Ubiquitin ligase (E3) that catalyzes p53 ubiquitination and proteasome-mediated degradation... Read More |