You Searched For: trans-4-Fluoro-L-proline


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Catalog Number: (C-2015.0025BA)
Supplier: Bachem Americas
Description: Sequence: Z-Hyp-OH


Supplier: Bachem Americas
Description: Sequence: Fmoc-Hyp-OH

Supplier: TCI America
Description: CAS Number: 13504-85-3
MDL Number: MFCD00037329
Molecular Formula: C13H15NO5
Molecular Weight: 265.27
Purity/Analysis Method: >98.0% (HPLC,T)
Form: Crystal
Melting point (°C): 107
Specific rotation [a]20/D: -54 deg (C=2, EtOH)

SDS

Catalog Number: (10109-584)
Supplier: Prosci
Description: PPIF is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.


Catalog Number: (75789-106)
Supplier: Prosci
Description: Cyclophilin C is an enzyme (EC 5.2.1.8) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but prolines unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.


Catalog Number: (10103-262)
Supplier: Prosci
Description: FKBP11 belongs to the FKBP family of peptidyl-prolyl cis/trans isomerases, which catalyze the folding of proline-containing polypeptides. The peptidyl-prolyl isomerase activity of FKBP proteins is inhibited by the immunosuppressant compounds FK506 and rapamycin.FKBP11 belongs to the FKBP family of peptidyl-prolyl cis/trans isomerases, which catalyze the folding of proline-containing polypeptides. The peptidyl-prolyl isomerase activity of FKBP proteins is inhibited by the immunosuppressant compounds FK506 and rapamycin (Rulten et al., 2006 [PubMed 16596453]).


Supplier: Bachem Americas
Description: Sequence: Z-Hyp(tBu)-OH

Catalog Number: (10426-328)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10426-388)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10426-390)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (76081-350)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10426-398)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10107-952)
Supplier: Prosci
Description: PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.


Catalog Number: (10426-396)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


Catalog Number: (10107-950)
Supplier: Prosci
Description: PPIE is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activityThe protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein contains a highly conserved cyclophilin (CYP) domain as well as an RNA-binding domain. It was shown to possess PPIase and protein folding activities and also exhibit RNA-binding activity. Three alternatively spliced transcript variants encoding distinct isoforms have been observed.


Catalog Number: (10426-394)
Supplier: Bioss
Description: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.


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