Explore
Validate
LearnABIN361829
antibody from antibodies-online
Targeting: P4HB
DSI, ERBA2L, GIT, P4Hbeta, PDI, PDIA1, PO4DB, PO4HB, PROHB
Western blotAntibody data
- Antibody Data
- Antigen structure
- References [9]
- Comments [0]
- Validations [0]
Submit
Validation data
Reference
Comment
Report error
- Product number
- ABIN361829 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361829, RRID:AB_10790388
- Product name
- anti-Prolyl 4-Hydroxylase, beta Polypeptide (P4HB) antibody
- Antibody type
- Polyclonal
- Antigen
- Rat PDI synthetic peptide conjugated to KLH
- Reactivity
- Human, Mouse, Rat, Bovine, Canine, Guinea Pig, Hamster, Porcine, Sheep, Simian, Xenopus
- Host
- Rabbit
- Isotype
- IgG
- Vial size
- 100 μL
- Storage
- -20°C
Submitted references Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.
Differential proteomic responses in hepatopancreas and adductor muscles of the green-lipped mussel Perna viridis to stresses induced by cadmium and hydrogen peroxide.
Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis.
Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function.
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Proteins of the PDI family: unpredicted non-ER locations and functions.
Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.
BiP and PDI cooperate in the oxidative folding of antibodies in vitro.
Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal.
Lauranzano E, Pozzi S, Pasetto L, Stucchi R, Massignan T, Paolella K, Mombrini M, Nardo G, Lunetta C, Corbo M, Mora G, Bendotti C, Bonetto V
Brain : a journal of neurology 2015 Apr;138(Pt 4):974-91
Brain : a journal of neurology 2015 Apr;138(Pt 4):974-91
Differential proteomic responses in hepatopancreas and adductor muscles of the green-lipped mussel Perna viridis to stresses induced by cadmium and hydrogen peroxide.
Leung PT, Wang Y, Mak SS, Ng WC, Leung KM
Aquatic toxicology (Amsterdam, Netherlands) 2011 Sep;105(1-2):49-61
Aquatic toxicology (Amsterdam, Netherlands) 2011 Sep;105(1-2):49-61
Protein disulfide isomerase is cleaved by caspase-3 and -7 during apoptosis.
Na KS, Park BC, Jang M, Cho S, Lee DH, Kang S, Lee CK, Bae KH, Park SG
Molecules and cells 2007 Oct 31;24(2):261-7
Molecules and cells 2007 Oct 31;24(2):261-7
Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function.
Schultz-Norton JR, McDonald WH, Yates JR, Nardulli AM
Molecular endocrinology (Baltimore, Md.) 2006 Sep;20(9):1982-95
Molecular endocrinology (Baltimore, Md.) 2006 Sep;20(9):1982-95
Regulation of NAD(P)H oxidase by associated protein disulfide isomerase in vascular smooth muscle cells.
Janiszewski M, Lopes LR, Carmo AO, Pedro MA, Brandes RP, Santos CX, Laurindo FR
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
The Journal of biological chemistry 2005 Dec 9;280(49):40813-9
Proteins of the PDI family: unpredicted non-ER locations and functions.
Turano C, Coppari S, Altieri F, Ferraro A
Journal of cellular physiology 2002 Nov;193(2):154-63
Journal of cellular physiology 2002 Nov;193(2):154-63
Role of extracellular molecular chaperones in the folding of oxidized proteins. Refolding of colloidal thyroglobulin by protein disulfide isomerase and immunoglobulin heavy chain-binding protein.
Delom F, Mallet B, Carayon P, Lejeune PJ
The Journal of biological chemistry 2001 Jun 15;276(24):21337-42
The Journal of biological chemistry 2001 Jun 15;276(24):21337-42
BiP and PDI cooperate in the oxidative folding of antibodies in vitro.
Mayer M, Kies U, Kammermeier R, Buchner J
The Journal of biological chemistry 2000 Sep 22;275(38):29421-5
The Journal of biological chemistry 2000 Sep 22;275(38):29421-5
Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal.
Yoshimori T, Semba T, Takemoto H, Akagi S, Yamamoto A, Tashiro Y
The Journal of biological chemistry 1990 Sep 15;265(26):15984-90
The Journal of biological chemistry 1990 Sep 15;265(26):15984-90
No comments: Submit comment
No validations: Submit validation data