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The protein encoded by PPIB is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. Additionally we are shipping Peptidylprolyl Isomerase B (Cyclophilin B) Antibodies (124) and Peptidylprolyl Isomerase B (Cyclophilin B) Kits (57) and many more products for this protein.
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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 (show PPIL2 Proteins) activity but shows altered cyclophilin B-protein (show LEPREL2 Proteins) 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 (show ADAMTS13 Proteins).
These data provide significant new mechanistic insight into the pathophysiology of Osteogenesis Imperfecta (show COL1A2 Proteins) and reveal how the members of the P3H1 (show LEPRE1 Proteins)/CRTAP (show CRTAP Proteins)/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 (show PPIE Proteins) (Ppib).
PPIB mutations and their associated phenotypes
observed changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP13 (FKBP2 (show FKBP2 Proteins)), FKBP19 (FKBP11 (show FKBP11 Proteins)), FKBP22 (FKBP14 (show FKBP14 Proteins)), FKBP23 (FKBP7 (show FKBP7 Proteins)), and FKBP65 (FKBP10 (show FKBP10 Proteins)), 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 (show LEPRE1 Proteins), CRTAP (show CRTAP Proteins), and PPIB genes. LEPRE1 (show LEPRE1 Proteins) 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 (show DDIT3 Proteins) protein degradation, suggesting that CypB may have an important role in the tight regulation of CHOP (show DDIT3 Proteins) under hypoxia.
These findings establish cyclophilin C (show PPIC Proteins) as an ER cyclophilin (show PPIA Proteins), demonstrate the novel involvement of cyclophilins B and C in ER redox homeostasis
Cyclophilin B is a novel MDM2 (show MDM2 Proteins) interacting partner.
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