| 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:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：HSPD1, also known as HSP60, is a member of the chaperonin family. HSPD1 may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：HSPD1, also known as HSP60, is a member of the chaperonin family. HSPD1 may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. It may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSPD1 gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. Defects in HSPD1 are a cause of spastic paraplegia autosomal dominant type 13 (SPG13). Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Defects in HSPD1 are the cause of leukodystrophy hypomyelinating type 4 (HLD4); also called mitochondrial HSP60 chaperonopathy or MitCHAP-60 disease. HLD4 is a severe autosomal recessive hypomyelinating leukodystrophy. HSPD1 is clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life... Read More | Purity≥ 92% SDS-PAGEActual molecular weight 15&17kDaFunctionChemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like Purity≥ 92% SDS-PAGEActual molecular weight 15&17kDaFunctionChemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis... Read More | Inquire |