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Human PDI Protein expressed in Escherichia coli (E. coli) - ABIN413737
Pendurthi, Ghosh, Mandal, Rao: Tissue factor activation: is disulfide bond switching a regulatory mechanism? in Blood 2007
Show all 2 Pubmed References
P4HB promotes hepatocellular carcinoma progression by down-regulating GRP78 (show HSPA5 Proteins) expression and subsequently promoting epithelial-to-mesenchymal transition.
analysis of antiplatelet activity of CxxC through binding to Cys400 in the PDI (show PADI1 Proteins) a0 domain, which can be further exploited as a model for sitedriven antithrombotic agent development
DIA1 (show CYB5R3 Proteins) was robustly secreted by physiological levels of arterial laminar shear in endothelial cells and supported alpha 5 integrin thiol oxidation.
Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates.
a mechanism of dual Ero1alpha regulation by dynamic redox interactions between PDI (show PADI1 Proteins) and the two Ero1alpha flexible loops that harbor the regulatory cysteines.
analysis of how redox affects human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol
These findings improve our understanding of PDI (show PADI1 Proteins)-protected aggregation of wild-type alpha-Syn and its H50Q familial mutant.
Association of P4HB polymorphisms with sporadic amyotrophic lateral sclerosis susceptibility in the Chinese Han population.
the effect of the endoplasmic reticulum chaperone protein disulfide isomerase (PDI) on beta-cell dysfunction, was examined.
Amyotrophic lateral sclerosis-linked PDIA1 mutations disrupt motor neuron connectivity.
Neutrophil surface PDI is important for alphaMbeta2 integrin-mediated adhesion of human neutrophils under shear and static conditions and for binding of soluble fibrinogen to activated alphaMbeta2 integrin.
Unfolded protein response caused by protein misfolding, may lead to PDI-dependent NOX activation and contribute to neurotoxicity in neurodegenerative diseases including ALS.
These results indicate that both endothelial and platelet beta3 integrins contribute to extracellular PDI (show PDIA3 Proteins) binding at the vascular injury site.
PDI (show PDIA3 Proteins) from endothelial cells is required for fibrin generation in vivo.
Protein disulfide isomerase (PDI) on the platelet surface is recognized by anti-dengue virus NS1 (show IVNS1ABP Proteins) antibodies.
Rotavirus-protein disulfide isomerase interaction was demonstrated in vitro as well as inMA104 cells and intestinal villi from suckling mice.
This gene encodes the beta subunit of prolyl 4-hydroxylase, a highly abundant multifunctional enzyme that belongs to the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, this enzyme is involved in hydroxylation of prolyl residues in preprocollagen. This enzyme is also a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds. Other known functions include its ability to act as a chaperone that inhibits aggregation of misfolded proteins in a concentration-dependent manner, its ability to bind thyroid hormone, its role in both the influx and efflux of S-nitrosothiol-bound nitric oxide, and its function as a subunit of the microsomal triglyceride transfer protein complex.
cellular thyroid hormone-binding protein
, collagen prolyl 4-hydroxylase beta
, glutathione-insulin transhydrogenase
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide
, prolyl 4-hydroxylase subunit beta
, protein disulfide isomerase family A, member 1
, protein disulfide isomerase-associated 1
, protein disulfide isomerase/oxidoreductase
, protein disulfide-isomerase
, protocollagen hydroxylase
, thyroid hormone-binding protein p55
, ER protein 59
, endoplasmic reticulum resident protein 59
, protein disulfide isomerase
, Protein disulfide isomerase (Prolyl 4-hydroxylase, beta polypeptide)
, PDI (E.C.126.96.36.199)
, cellular thyroid hormone binding protein
, prolyl 4-hydroxylase beta polypeptide
, prolyl 4-hydroxylase, beta subunit
, Cellular thyroid hormone-binding protein
, Prolyl 4-hydroxylase subunit beta
, multifunctional thyroid hormone binding protein
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide (protein disulfide isomerase-associated 1)
, procollagen-proline, 2-oxoglutarate 4-dioxygenase (proline 4-hydroxylase), beta polypeptide (protein disulfide isomerase; thyroid hormone binding protein p55)
, retina cognin
, protein disulphide isomerase PDI
, prolyl 4-hydroxylase, beta polypeptide