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Catalog Number: (10392-078)
Supplier: Bioss
Description: This gene encodes an enzyme, consisting of two identical proteins, which catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in this gene are associated with triosephosphate isomerase deficiency. Pseudogenes have been identified on chromosomes 1, 4, 6 and 7. Alternative splicing results in multiple transcript variants. [provided by RefSeq]


Catalog Number: (10103-904)
Supplier: Prosci
Description: Protein disulfide isomerases, such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to play a role in folding of disulfide-bonded proteins.Protein disulfide isomerases (EC 5.3.4.1), such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to play a role in folding of disulfide-bonded proteins (Hayano and Kikuchi, 1995 [PubMed 7590364]).


Catalog Number: (10392-076)
Supplier: Bioss
Description: This gene encodes an enzyme, consisting of two identical proteins, which catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in this gene are associated with triosephosphate isomerase deficiency. Pseudogenes have been identified on chromosomes 1, 4, 6 and 7. Alternative splicing results in multiple transcript variants. [provided by RefSeq]


Catalog Number: (77437-914)
Supplier: Bioss
Description: Associates with the ryanodine receptor (RYR-2) in cardiac muscle sarcoplasmic reticulum and may play a unique physiological role in excitation-contraction coupling in cardiac muscle. There are four molecules of FKBP12.6 per heart muscle RYR. Has the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10461-782)
Supplier: Bioss
Description: Pseudouridination is the isomerization of uridine to pseudouridine. It is the most common posttranscriptional nucleotide modification found in RNA. It is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones which facilitate the correct folding and assembly of tRNAs.


Supplier: Thermo Scientific
Description: The Thermo Scientific™ GlycanPac™ AXR-1 column is a high-performance, silica-based HPLC column for the simultaneous separation of glycans by charge, isomerism, and size. It is designed to provide industry-leading resolution with unique selectivities for biologically important glycans, either labeled or native, using either fluorescence and/or mass spectrometry (MS) detection.

Catalog Number: (10814-208)
Supplier: Prosci
Description: Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner.


Catalog Number: (10072-330)
Supplier: Prosci
Description: This protein is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10092-650)
Supplier: Proteintech
Description: PPIH(Peptidyl-prolyl cis-trans isomerase H) is also named as CYP20, CYPH and belongs to cyclophilin-type PPIase family, PPIase H subfamily.It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may act as a chaperone.


Catalog Number: (10069-756)
Supplier: Prosci
Description: FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ("psi") residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.


Catalog Number: (10090-370)
Supplier: Proteintech
Description: MPI(mannose-6-phosphate isomerase) is also named as PMI1 and belongs to the mannose-6-phosphate isomerase type 1 family. It is a zinc metalloenzyme that catalyzes the reversible isomerization of mannose-6-phosphate and fructose-6-phosphate. MPI plays a critical role in maintaining the supply of D-mannose derivatives, which are required for most glycosylation reactions. This proterin has 2 isoforms produced by alternative splicing.


Catalog Number: (10461-764)
Supplier: Bioss
Description: Pseudouridination is the isomerization of uridine to pseudouridine. It is the most common posttranscriptional nucleotide modification found in RNA. It is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones which facilitate the correct folding and assembly of tRNAs.


Catalog Number: (10461-778)
Supplier: Bioss
Description: Pseudouridination is the isomerization of uridine to pseudouridine. It is the most common posttranscriptional nucleotide modification found in RNA. It is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones which facilitate the correct folding and assembly of tRNAs.


Catalog Number: (10461-786)
Supplier: Bioss
Description: Pseudouridination is the isomerization of uridine to pseudouridine. It is the most common posttranscriptional nucleotide modification found in RNA. It is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones which facilitate the correct folding and assembly of tRNAs.


Catalog Number: (10092-644)
Supplier: Proteintech
Description: PPID(Peptidyl-prolyl cis-trans isomerase D) is also named as CYP40, CYPD and belongs to the cyclophilin-type PPIase family,which accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. The inactivation of the Ppid gene rescued the disease phenotype of Col6a1 deficiency .


Catalog Number: (76116-612)
Supplier: Bioss
Description: Pseudouridination is the isomerization of uridine to pseudouridine. It is the most common posttranscriptional nucleotide modification found in RNA. It is essential for biologic functions such as spliceosome biogenesis. Pseudouridylate synthases, such as PUS10, catalyze pseudouridination of structural RNAs, including transfer, ribosomal, and splicing RNAs. These enzymes also act as RNA chaperones which facilitate the correct folding and assembly of tRNAs.


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