| Description | CTSO Human Pre-designed siRNA Set A contains three designed siRNAs for CTSO gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CTSO siRNA-1: 5 nmol (HPLC) CTSO siRNA-2: 5 nmol (HPLC) CTSO siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 CTSO Human Pre-designed siRNA Set A contains three designed siRNAs for CTSO gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CTSO siRNA-1: 5 nmol (HPLC) CTSO siRNA-2: 5 nmol (HPLC) CTSO 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 | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc | Purity>95% SDS-PAGE.FunctionB Cell Activating Factor Receptor (BAFF-R), also named tumor necrosis factor receptor superfamily member 13C, is a member of the TNFR superfamily. It is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ Purity>95% SDS-PAGE.FunctionB Cell Activating Factor Receptor (BAFF-R), also named tumor necrosis factor receptor superfamily member 13C, is a member of the TNFR superfamily. It is highly expressed in spleen, lymph node, and resting B cells and to some extent in activated B cells, resting CD4+ cells and peripheral blood leukocytes. BAFF receptor is a type III transmembrane protein containing a single extracellular phenylalanine-rich domain and binds with high specificity to BAFF (TNFSF13B). It enhances B-cell survival in vitro and is a regulator of the peripheral B-cell population. BAFF receptor/BAFF signaling plays a critical role in B cell survival and maturation... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein,Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein, released actively following cytokine stimulation as well as passively during cell death. It is the prototypic damage-associated molecular pattern (DAMP) molecule and has been implicated in several inflammatory disorders. HMGB1 signals via the receptor for advanced glycation end-product (RAGE) and members of the toll-like receptor (TLR) family. The most prominent HMGB1 protein and mRNA expression arthritis are present in pannus regions, where synovial tissue invades articular cartilage and bone. HMGB1 promotes the activity of proteolytic enzymes, and osteoclasts need HMGB1 for functional maturation. As a non-histone nuclear protein, HMGB1 has a dual function. Inside the cell, HMGB1 binds DNA, regulating transcription, and determining chromosomal architecture. Outside the cell, HMGB1 can serve as an alarmin to activate the innate system and mediate a wide range of physiological and pathological responses. Extracellular HMGB1 represents an optimal " necrotic marker" selected by the innate immune system to recognize tissue damage and initiate reparative responses. However, extracellular HMGB1 also acts as a potent pro-inflammatory cytokine that contributes to the pathogenesis of diverse inflammatory and infectious disorders. HMGB1 has been successfully therapeutically targeted in multiple preclinical models of infectious and sterile diseases including arthritis. As shown in studies on patients as well as animal models, HMGB1 can play an important role in the pathogenesis of the rheumatic disease, including rheumatoid arthritis, systemic lupus erythematosus, and polymyositis among others. Besides, enhanced postmyocardial infarction remodeling in type 1 diabetes mellitus was partially mediated by HMGB1 activation... Read More | 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 |