| Description | Microbial derived chondroitin sulfate (CS)/dermatan sulfate (DS) sugar chain degrading enzymes (CSases) belong to polysaccharide lyases, which break the β -1,4-glycosidic bond between N-acetylglucosamine (GalNAc) and hexuronic acid (GlcUA/IdoUA) through a b-elimination reaction. At the same Microbial derived chondroitin sulfate (CS)/dermatan sulfate (DS) sugar chain degrading enzymes (CSases) belong to polysaccharide lyases, which break the β -1,4-glycosidic bond between N-acetylglucosamine (GalNAc) and hexuronic acid (GlcUA/IdoUA) through a b-elimination reaction. At the same time, unsaturated double bonds are formed between the C4 and C5 carbon atoms of the uronic acid, which have characteristic absorption at 232 nm and can be conveniently used for oligosaccharide product analysis and detection. Commercialized CSases include CSase ABC from Proteus vulgaris, which can simultaneously degrade CS, DS, and HA. In fact, CSase ABC is a mixture of two enzymes, with CSase ABCI being a CS/DS endonuclease and CSase ABCII being a non reducing end exonuclease of CS/DS; CSase ACI and B from Flavobacterium heparinum, where CSase ACI is a CS and HA specific endonuclease, while the latter is a DS specific endonuclease; The CSase ACII from Arthrobacter auricens is another CS and HA specific degrading enzyme, but it is an exonuclease that can effectively cleave the enzyme labeled with tetrasaccharides at the reducing end of CS oligosaccharides after being fluorescently labeled. Therefore, it is particularly useful in CS oligosaccharides enzymatic sequencing. CS/DS lyase is not only an important tool enzyme for studying the structure-activity relationship of CS/DS and preparing CS/DS oligosaccharides, but also has significant clinical application value in the treatment of central nervous system injuries. We can provide customers with various CSases with different substrate selectivity, substrate degradation modes, and specifications according to their needs, meeting various needs such as CS/DS structural and functional analysis, product quality testing, heparin/heparan sulfate production and purification, and large-scale enzymatic hydrolysis preparation of CS and DS functional oligosaccharides... Read More | 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 | 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 | Purity≥95% SDS-PAGE.Endotoxin level<0.1 EU/µgFunctionMediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature Purity≥95% SDS-PAGE.Endotoxin level<0.1 EU/µgFunctionMediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration. Serves as a receptor for poliovirus attachment to target cells. May play a role in axonal transport of poliovirus, by targeting virion-PVR-containing endocytic vesicles to the microtubular network through interaction with DYNLT1. This interaction would drive the virus-containing vesicle to the axonal retrograde transport... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:BIRC5, also known as Survivin and EPR-1, is a member of theIAP family. IAP family members usually contain multiple baculovirus IAP repeat (BIR) domains, but BIRC5 has only a single BIR domain. It is expressed cell cycle-dependently and highly expressed at mitosis. As a multitasking protein, BIRC5 has dual roles in promoting cell proliferation and preventing apoptosis. Survivin is a component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Survivin acts as an important regulator of the localization of this complex. It may counteract a default induction of apoptosis in G2/M phase... Read More |