276 Results for: "Manganesebis(trifluoromethylsulphonyl)imide"

Supplier: Apollo Scientific

1-Butyl-3-Vinylimidazolium Bis((Trifluorompropyl)Sulfonyl)Imide 100g pack 1 * 100 g

Supplier: Bioss

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.

Supplier: ProSci Inc.

PPWD1 is a putative peptidylprolyl isomerase (PPIase). PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPWD1 may be involved in pre-mRNA splicing.

Supplier: USP

rac-Pregabalin Imide Dimer Amide (25 mg) (3-((3-(aminomethyl)-5-methylhexanamido)methyl)-5-methylhexanoic acid) 1 * 25 mg

Supplier: Thermo Fisher Scientific

Cross linkers are used for the identification of near-neighbour protein relationships and ligand-receptor interactions. Homobifunctional, amine-reactive NHS esters or imidates, and heterobifunctional, amine-reactive, photoactivatable phenyl azides are the most commonly used crosslinkers for these applications.

Supplier: Thermo Fisher Scientific

Cross linkers are used for the identification of near-neighbour protein relationships and ligand-receptor interactions. Homobifunctional, amine-reactive NHS esters or imidates, and heterobifunctional, amine-reactive, photoactivatable phenyl azides are the most commonly used crosslinkers for these applications.

Supplier: Thermo Fisher Scientific

Cross linkers are used for the identification of near-neighbour protein relationships and ligand-receptor interactions. Homobifunctional, amine-reactive NHS esters or imidates, and heterobifunctional, amine-reactive, photoactivatable phenyl azides are the most commonly used crosslinkers for these applications.

Supplier: Thermo Fisher Scientific

Cross linkers are used for the identification of near-neighbour protein relationships and ligand-receptor interactions. Homobifunctional, amine-reactive NHS esters or imidates, and heterobifunctional, amine-reactive, photoactivatable phenyl azides are the most commonly used cross linkers for these applications.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyse the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyse the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Supplier: Bioss

Peptidyl-prolyl cis-trans isomerase (PPIL1) 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 HIV1 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.

Supplier: USP

Desethylazilsartan Open Ring (25 mg) (3-((2'-(N-hydroxycarbamimidoyl)-[1,1'-biphenyl]-4-yl)methyl)-2-oxo-2,3-dihydro-1H-benzo[d]imid azole-4-carboxylic acid) 1 * 25 mg

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

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.

Supplier: ProSci Inc.

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 catalyses the cis-trans isomerisation 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.

Supplier: Thermo Fisher Scientific

2-[N,N-Bis(trifluoromethanesulphonyl)amino]-5-chloropyridine

Supplier: ProSci Inc.

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.

Supplier: Apollo Scientific

2-[N,N-Bis(trifluoromethanesulphonyl)amino]-5-chloropyridine

Supplier: Bioworld Technology

The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-tr ans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. 1 * 100 µG