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Cow (Bovine) Monoclonal PDI Primary Antibody for BP, ELISA - ABIN152676
Courageot, Fenouillet, Bastiani, Miquelis: Intracellular degradation of the HIV-1 envelope glycoprotein. Evidence for, and some characteristics of, an endoplasmic reticulum degradation pathway. in European journal of biochemistry 1999
Show all 17 Pubmed References
Dog (Canine) Monoclonal PDI Primary Antibody for IF, WB - ABIN968267
Jenne, Frey, Brugger, Wieland: Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway. in The Journal of biological chemistry 2002
Show all 5 Pubmed References
Dog (Canine) Monoclonal PDI Primary Antibody for IF, WB - ABIN968268
Schlegel, Arvan, Lisanti: Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum. in The Journal of biological chemistry 2001
Show all 5 Pubmed References
Cow (Bovine) Polyclonal PDI Primary Antibody for ICC, IF - ABIN4344553
Safran, Farwell, Leonard: Thyroid hormone-dependent redistribution of the 55-kilodalton monomer of protein disulfide isomerase in cultured glial cells. in Endocrinology 1992
Show all 3 Pubmed References
Cow (Bovine) Polyclonal PDI Primary Antibody for ICC, IF - ABIN361829
Na, Park, Jang, Cho, Lee, Kang, Lee, Bae, Park: Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis. in Molecules and cells 2007
Show all 9 Pubmed References
Hamster Monoclonal PDI Primary Antibody for ICC, FACS - ABIN269364
Jun, Lee, Song, Mansfield, Chou: G-CSF improves murine G6PC3-deficient neutrophil function by modulating apoptosis and energy homeostasis. in Blood 2011
Show all 2 Pubmed References
Human Polyclonal PDI Primary Antibody for ELISA, WB - ABIN188849
Uehara, Nakamura, Yao, Shi, Gu, Ma, Masliah, Nomura, Lipton: S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. in Nature 2006
Cow (Bovine) Polyclonal PDI Primary Antibody for IHC, WB - ABIN2783246
Ewing, Chu, Elisma, Li, Taylor, Climie, McBroom-Cerajewski, Robinson, OConnor, Li, Taylor, Dharsee, Ho, Heilbut, Moore, Zhang, Ornatsky, Bukhman, Ethier, Sheng, Vasilescu, Abu-Farha, Lambert, Duewel et al.: Large-scale mapping of human protein-protein interactions by mass spectrometry. ... in Molecular systems biology 2007
Human Monoclonal PDI Primary Antibody for ELISA, ICC - ABIN4347867
Limoge, Safina, Beattie, Kapus, Truskinovsky, Bakin: Tumor-fibroblast interactions stimulate tumor vascularization by enhancing cytokine-driven production of MMP9 by tumor cells. in Oncotarget 2017
DIA1 (show CYB5R3 Antibodies) 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 Antibodies) 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 Antibodies)-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.
direct binding of PDIA1 to VWF (show VWF Antibodies), is reported.
Selective sequestration of PDI1A in a calcium depletion-mediated complex with the abundant chaperone calreticulin (show CALR Antibodies) attenuates the effective concentration of this major lumenal thiol oxidant.
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 Antibodies) binding at the vascular injury site.
PDI (show PDIA3 Antibodies) 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 Antibodies) 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.184.108.40.206)
, 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