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AB198461

Recombinant Human Cyclophilin 40 protein (GST tag N-Terminus)

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Recombinant Human Cyclophilin 40 protein (GST tag N-Terminus) is a Human Full Length protein, in the 2 to 370 aa range, expressed in Escherichia coli, with >73%, suitable for SDS-PAGE.

View Alternative Names

CYP40, CYPD, PPID, Peptidyl-prolyl cis-trans isomerase D, PPIase D, 40 kDa peptidyl-prolyl cis-trans isomerase, Cyclophilin-40, Cyclophilin-related protein, Rotamase D, CYP-40

1 Images
SDS-PAGE - Recombinant Human Cyclophilin 40 protein (GST tag N-Terminus) (AB198461)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human Cyclophilin 40 protein (GST tag N-Terminus) (AB198461)

4-20% SDS-PAGE analysis of ab198461 with Coomassie staining.

Lane 1 : 3.7 μg ab198461
Lane 2 : Protein marker

Key facts

Purity

>73% SDS-PAGE

Expression system

Escherichia coli

Tags

GST tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q08752

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.49% Glutathione, 0.02% Potassium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Sequence info

[{"sequence":"MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLEVLFQGPLGSSHPSPQAKPSNPSNPRVFFDVDIGGERVGRIVLELFADIVPKTAENFRALCTGEKGIGHTTGKPLHFKGCPFHRIIKKFMIQGGDFSNQNGTGGESIYGEKFEDENFHYKHDREGLLSMANAGRNTNGSQFFITTVPTPHLDGKHVVFGQVIKGIGVARILENVEVKGEKPAKLCVIAECGELKEGDDGGIFPKDGSGDSHPDFPEDADIDLKDVDKILLITEDLKNIGNTFFKSQNWEMAIKKYAEVLRYVDSSKAVIETADRAKLQPIALSCVLNIGACKLKMSNWQGAIDSCLEALELDPSNTKALYRRAQGWQGLKEYDQALADLKKAQGIAPEDKAIQAELLKVKQKIKAQKDKEKAVYAKMFA","proteinLength":"Full Length","predictedMolecularWeight":"68 kDa","actualMolecularWeight":null,"aminoAcidEnd":370,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q08752","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

General info

Function

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed : 11350175, PubMed : 20676357). Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR : ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines.. (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release.

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Subcellular localisation

Nucleus

Product protocols

Target data

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed : 11350175, PubMed : 20676357). Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR : ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines.. (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release.
See full target information PPID

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