| Description | α Amylase-IN-1 (Compound 11) is an α-Amylase inhibitor with an IC 50 value of 0.5509 µM. α Amylase-IN-1 has antioxidant activity with an IC 50 value of 53.49 µM for scavenging DPPH free radicals. IC 50 can be used in the study of diabetes and oxidative stress-related α Amylase-IN-1 (Compound 11) is an α-Amylase inhibitor with an IC 50 value of 0.5509 µM. α Amylase-IN-1 has antioxidant activity with an IC 50 value of 53.49 µM for scavenging DPPH free radicals. IC 50 can be used in the study of diabetes and oxidative stress-related diseases... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Major histocompatibility complex, class II, DR alpha (HLA-DRA) belongs to the MHC class II family. HLA-DRA binds peptides derived from antigens which access the endocytic route of antigen presenting cells (APC) Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Major histocompatibility complex, class II, DR alpha (HLA-DRA) belongs to the MHC class II family. HLA-DRA binds peptides derived from antigens which access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for identification by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mainly by degradation of proteins which access the endocytic route, where they are processed by lysosomal proteases and other hydrolases... 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 | 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 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 | Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal Stem Cell Factor (SCF) which binds to the c-Kit receptor is produced by fibroblasts and endothelial cells. The soluble and transmembrane forms of the protein are formed by alternative splicing of the same RNA transcript and the presence of both soluble and transmembrane It is required for normal hematopoietic function and plays an important role in hematopoiesis, spermatogenesis, and melanogenesis. It also promotes mast cell adhesion, migration, proliferation, and survival. Human SCF manifests low activity on murine cells, while murine and rat SCF are fully active on human cells. Recombinant murine SCF is an 18.4kDa polypeptide containing 165 amino acid residues.Purity＞97% (SDS-PAGE,HPLC)FunctionLigand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.Post-translationalA soluble form (sKITLG) is produced by proteolytic processing of isoform 1 in the extracellular domain. Found in two differentially glycosylated forms, LMW-SCF and HMW-SCF. LMW-SCF is fully N-glycosylated at Asn-145, partially N-glycosylated at Asn-90, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97 or Asn-118. HMW-SCF is N-glycosylated at Asn-118, Asn-90 and Asn-145, O-glycosylated at Ser-167, Thr-168 and Thr-180, and not glycosylated at Asn-97. A soluble form exists as a cleavage product of the extracellular domain... Read More |