异构酶 (Isomerases,EC 5)

Expression system: E. coli
Length: 1-165, Full Length
Activity: Not Tested

Peroxisomal acyl-coenzyme A oxidase 1(ACOX1 or AOX) is the first enzyme of the fatty acid beta-oxidation pathway and belongs to the Acyl-CoA oxidase family. Human liver peroxisomes contain two acyl-CoA oxidases, namely, palmitoyl-CoA oxidase (ACOX1 AOX) and a branched chain acyl-CoA oxidase. The palmitoyl-CoA oxidase (ACOX1 AOX) oxidizes the CoA esters of straight chain fatty acids and prostaglandins and donates electrons directly to molecular oxygen, thereby producing H2O2. Human ACOX1 AOX is a protein of 661-amino acids, including the carboxyl-terminal sequence(Ser-Lys-Leu) known as a minimal peroxisome-targeting signal. Human ACOX1 AOX, the first and rate-limiting enzyme of the peroxisomal β-oxidation pathway, has two isoforms including ACOX1a and ACOX1b, transcribed from a single gene. The human ACOX1b isoform is more effective than the ACOX1a isoform in reversing the Acox1 null phenotype in the mouse partly because of the Substrate utilization differences.

Expression system: HEK293 Cells
Length: 1-190, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 2-732, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-340, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 25-505, Full Length of Mature Protein
Activity: Not Tested

Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.

Expression system: E. coli
Length: 2-875, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 415-804, partial
Activity: Not Tested

FKBP12 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 12.7 kDa and the accession number is P26883.

PIN1 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 20.3 kDa and the accession number is Q13526-1.

Peptidyl-prolyl cis-trans isomerase A is a cytoplasm protein which belongs to the cyclophilin-type PPIase family and PPIase A subfamily. Cyclophilins(CyPs) are a family of proteins found in organisms ranging from prokaryotes to humans. These molecules exhibit peptidyl-prolyl isomerase activity, suggesting that they influence the conformation of proteins in cells. Cyclophilin A accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Cyclophilin A can interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions.

APOA1BP, now renamed NAXE, encodes an epimerase essential in the cellular metabolite repair for NADHX and NADPHX. The enzyme catalyzes the epimerization of NAD(P)HX, thereby avoiding the accumulation of toxic metabolites.Pathogenic biallelic mutations in NAXE in children from four families with (sub-) acute-onset ataxia, cerebellar edema, spinal myelopathy, and skin lesions.

Prostaglandin D2 Synthase Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 20.3 kDa and the accession number is A6JT70.

Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.

Protein Disulfide-Isomerase A6 (PDIA6) is a 48.5kDa protein that belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. The PDIA6 expressed in platelets, its functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6 is part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1. PDIA6 also plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

Triose-phosphate isomerase, also named Triose-phosphate isomerase, TPI and TIM, is an enzyme that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI deficiency is an autosomal recessive disorder and the most severe clinical disorder of glycolysis. Triose phosphate isomerase deficiency is associated with neonatal jaundice, chronic hemolytic anemia, progressive neuromuscular dysfunction, cardiomyopathy and increased susceptibility to infection and characterized by chronic hemolytic anemia.

Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the GST superfamily and Sigma family. HPGDS contains one GST C-terminal domain and one GST N-terminal domain. HPGDS is highly expressed in adipose tissue, macrophages, and placenta, and it exists in the form of homodimer in living body. HPGDS is a cytosolic enzyme that isomerizes PGH(2). HPGDS is a bifunctional enzyme that catalyzes both the conversion of PGH2 to PGD2 and also shows low glutathione-peroxidase activity towards cumenehydroperoxide.

Expression system: E. coli
Length: 2-63, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-362, Partial
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 1-432, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-301, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 2-544, Full Length of Mature Protein
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 20-509, Full Length of Mature Protein
Activity: Not Tested