| 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 | Inquire | Inquire | 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>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the Purity>95% SDS-PAGE.FunctionReceptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity... Read More |