PPIC Protein (AA 31-182) (TRX tag,His tag)
Quick Overview for PPIC Protein (AA 31-182) (TRX tag,His tag) (ABIN1096479)
Target
See all PPIC ProteinsProtein Type
Origin
Source
Purity
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Protein Characteristics
- AA 31-182
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Purification tag / Conjugate
- This PPIC protein is labelled with TRX tag,His tag.
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Purpose
- Recombinant Human Cyclophilin C/PPIase C/PPIC (N-Trx, 6His)
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Sequence
- MSDKIIHLTD DSFDTDVLKA DGAILVDFWA EWCGPCKMIA PILDEIADEY QGKLTVAKLN IDQNPGTAPK YGIRGIPTLL LFKNGEVAAT KVGALSKGQL KEFLDANLAG SGSGHMHHHH HHSSGLVPRG SGMKETAAAK FERQHMDSPD LGTDDDDKAM AKRGPSVTAK VFFDVRIGDK DVGRIVIGLF GKVVPKTVEN FVALATGEKG YGYKGSKFHR VIKDFMIQGG DITTGDGTGG VSIYGETFPD ENFKLKHYGI GWVSMANAGP DTNGSQFFIT LTKPTWLDGK HVVFGKVIDG MTVVHSIELQ ATD
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Characteristics
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Recombinant Human Cyclophilin C/PPIase C/PPIC (N-Trx, 6His)
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Sterility
- 0.2 μm filtered
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Endotoxin Level
- Less than 0.1 ng/μg (1 IEU/μg) as determined by LAL test
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Restrictions
- For Research Use only
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Format
- Liquid
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Reconstitution
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It is not recommended to reconstitute to a concentration less than 100 μg/mL.
Dissolve the lyophilized protein in ddH2O.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. -
Buffer
- Supplied as a 0.2 μm filtered solution of 20 mM PB, 150 mM NaCl, 10 % Glycerol, pH 7.4.
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Handling Advice
- Always centrifuge tubes before opening. Do not mix by vortex or pipetting.
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Storage
- -80 °C
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Storage Comment
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Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles. -
Expiry Date
- 6 months
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- PPIC (Peptidylprolyl Isomerase C (Cyclophilin C) (PPIC))
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Alternative Name
- Cyclophilin C
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Background
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Recombinant Human Cyclophilin C/CYPC is produced by our E. coli expression system. The target protein is expressed with sequence (Trp131-Asp182) of Human CYPC fused with a His tag at the N-terminus.
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 AA 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 AAs 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. -
Molecular Weight
- 33.78 kDa
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UniProt
- P45877
Target
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