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The protein encoded by PPIB is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. Zusätzlich bieten wir Ihnen Peptidylprolyl Isomerase B (Cyclophilin B) Antikörper (123) und Peptidylprolyl Isomerase B (Cyclophilin B) Kits (57) und viele weitere Produktgruppen zu diesem Protein an.
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Human PPIB Protein expressed in Human Cells - ABIN2003709
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 2006
Show all 3 Pubmed References
Data indicate that the mutation in cyclophilin B (CypB) locally rearranges the flexible N-terminal end of the polypeptide chain and also makes it more rigid.
Mutation in cyclophilin B that causes hyperelastosis cutis in American Quarter Horse does not affect peptidylprolyl cis-trans isomerase (zeige PPIL2 Proteine) activity but shows altered cyclophilin B-protein (zeige LEPREL2 Proteine) interactions and affects collagen folding
The prevalence of a previously described mutation in cyclophilin B (a causal candidate gene for hereditary equine regional dermal asthenia) among Quarter Horses in France was determined to be 1.6%.
A missense mutation in cyclophilin B (PPIB) is reported as a novel, causal candidate gene for hereditary equine regional dermal asthenia (HERDA).
These studies demonstrate novel consequences of the indirect regulatory effect of CyPB on collagen hydroxylation, impacting collagen glycosylation, crosslinking and fibrillogenesis
An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro.
Cyclophilin B activity regulated secretion and activity of ADAMTS13 (zeige ADAMTS13 Proteine).
These data provide significant new mechanistic insight into the pathophysiology of Osteogenesis Imperfecta (zeige COL1A2 Proteine) and reveal how the members of the P3H1 (zeige LEPRE1 Proteine)/CRTAP (zeige CRTAP Proteine)/CypB complex interact to direct proper formation of collagen and bone.
These results suggest that immunophilins are involved in the complex protein networks operating at the presynaptic level and implicate the interaction between cyclophilin B and synapsins in presynaptic function.
The protein identified was cyclophilin (zeige PPIE Proteine) (Ppib).
cyclophilin B (CYPB) functions in protecting cells against aldosterone-induced oxidative stress, endoplasmic reticulum stress (ERS) and tubular cell injury via its peptidyl-prolyl cis-trans isomerase (PPIase (zeige PPIL1 Proteine)) activity.
PPIB mutations and their associated phenotypes
observed changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP13 (FKBP2 (zeige FKBP2 Proteine)), FKBP19 (FKBP11 (zeige FKBP11 Proteine)), FKBP22 (FKBP14 (zeige FKBP14 Proteine)), FKBP23 (FKBP7 (zeige FKBP7 Proteine)), and FKBP65 (FKBP10 (zeige FKBP10 Proteine)), due to posttranslational modifications of proline residues in the substrate.
The data suggest that overexpressed CypB protects neuronal cells from MPP+-induced dopaminergic neuronal cell death
This study enhances our knowledge about the mutational pattern of the LEPRE1 (zeige LEPRE1 Proteine), CRTAP (zeige CRTAP Proteine), and PPIB genes. LEPRE1 (zeige LEPRE1 Proteine) should be the first gene analyzed in mutation detection studies in patients with recessive OI.
Over-expression of CypB enhances HIV infection by increasing nuclear import of viral DNA.
Cyclophilin B has a high diagnostic value for stomach cancer and its downregulation can effectively inhibit the growth of stomach cancer cells. Thus, cyclophilin B may be a potential therapeutic target for stomach cancer treatment
The extracellular portion of cyclophilin B probably plays an important role in human diseases associated with acute or chronic inflammation
Findings demonstrate that CypB prevents hypoxia-induced cell death through modulation of ubiquitin-mediated CHOP (zeige DDIT3 Proteine) protein degradation, suggesting that CypB may have an important role in the tight regulation of CHOP (zeige DDIT3 Proteine) under hypoxia.
These findings establish cyclophilin C (zeige PPIC Proteine) as an ER cyclophilin (zeige PPIA Proteine), demonstrate the novel involvement of cyclophilins B and C in ER redox homeostasis
Cellular CypB was confirmed to be significantly up-regulated in the Orf virus-infected MDBK cells at an early phase of infection, which could effectively facilitate the replication of Orf virus.
The protein encoded by this gene is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression. Variants have been identified in this protein that give rise to recessive forms of osteogenesis imperfecta.
, peptidylprolyl isomerase B
, peptidylprolyl isomerase B (cyclophilin B)
, PPIase B
, peptidyl-prolyl cis-trans isomerase B
, Peptidyl-prolyl cis-trans isomerase B
, rotamase B
, cyclophilin-like protein