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  • 产品名称：PeptidylprolylIsomeraseB(CyclophilinB)(PPIB)(AA34-212)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
PeptidylprolylIsomeraseB(CyclophilinB)(PPIB)(AA34-212)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 20.7 kDa. The protein migrates as 22 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
Background Peptidyl-prolyl cis-trans isomerase B (PPIB or PPIase B) is also known as Cyclophilin B (CYPB), Rotamase B, S-cyclophilin (SCYLP), is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum, which belongs to the cyclophilin-type PPIase family and PPIase B subfamily. PPIB / CYPB contains one PPIase cyclophilin-type domain. PPIases accelerate the folding of proteins and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Molecular Weight 20.7 kDa
NCBI Accession NP_000933
UniProt P23284
Research Area Signaling
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for Peptidylprolyl Isomerase B (Cyclophilin B) (PPIB) (AA 34-212) (Active) protein (His tag) (ABIN2181661) Human PPIB, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained ove...
Background publications Chi, Valencia, Hu, Watabe, Yamaguchi, Mangini, Huang, Canfield, Cheng, Yang, Abe, Yamagishi, Shabanowitz, Hearing, Wu, Appella, Hunt: "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." in: Journal of proteome research, Vol. 5, Issue 11, pp. 3135-44, 2006 (PubMed).

Arber, Krause, Caroni: "s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin." in: The Journal of cell biology, Vol. 116, Issue 1, pp. 113-25, 1992 (PubMed).