ABIN361815
antibody from antibodies-online
Targeting: PDIA3
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC
Antibody data
- Antibody Data
- Antigen structure
- References [13]
- Comments [0]
- Validations
- Western blot [1]
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- Product number
- ABIN361815 - Provider product page
- Provider
- antibodies-online
- Proper citation
- Antibodies-Online Cat#ABIN361815, RRID:AB_10769566
- Product name
- anti-Protein Disulfide Isomerase Family A, Member 3 (PDIA3) antibody
- Antibody type
- Monoclonal
- Description
- Protein G Purified
- Reactivity
- Human, Mouse, Rat, Bovine, Canine, Guinea Pig, Hamster, Porcine, Rabbit, Simian
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- Map-ERp57
- Vial size
- 200 μg
- Storage
- -20°C
Submitted references Interaction with the effector dynamin-related protein 1 (Drp1) is an ancient function of Rab32 subfamily proteins.
Palmitoylation is the switch that assigns calnexin to quality control or ER Ca2+ signaling.
The green fluorescent protein as an efficient selection marker for Agrobacterium tumefaciens-mediated transformation in Hevea brasiliensis (Müll. Arg).
In and out of the ER: protein folding, quality control, degradation, and related human diseases.
Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle.
Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum.
ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.
ERp57 binds competitively to protein disulfide isomerase and calreticulin.
Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors.
Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading.
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins.
Ortiz-Sandoval CG, Hughes SC, Dacks JB, Simmen T
Cellular logistics 2014 Oct-Dec;4(4):e986399
Cellular logistics 2014 Oct-Dec;4(4):e986399
Palmitoylation is the switch that assigns calnexin to quality control or ER Ca2+ signaling.
Lynes EM, Raturi A, Shenkman M, Ortiz Sandoval C, Yap MC, Wu J, Janowicz A, Myhill N, Benson MD, Campbell RE, Berthiaume LG, Lederkremer GZ, Simmen T
Journal of cell science 2013 Sep 1;126(Pt 17):3893-903
Journal of cell science 2013 Sep 1;126(Pt 17):3893-903
The green fluorescent protein as an efficient selection marker for Agrobacterium tumefaciens-mediated transformation in Hevea brasiliensis (Müll. Arg).
Leclercq J, Lardet L, Martin F, Chapuset T, Oliver G, Montoro P
Plant cell reports 2010 May;29(5):513-22
Plant cell reports 2010 May;29(5):513-22
In and out of the ER: protein folding, quality control, degradation, and related human diseases.
Hebert DN, Molinari M
Physiological reviews 2007 Oct;87(4):1377-408
Physiological reviews 2007 Oct;87(4):1377-408
Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle.
Soldà T, Garbi N, Hämmerling GJ, Molinari M
The Journal of biological chemistry 2006 Mar 10;281(10):6219-26
The Journal of biological chemistry 2006 Mar 10;281(10):6219-26
Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum.
Williams DB
Journal of cell science 2006 Feb 15;119(Pt 4):615-23
Journal of cell science 2006 Feb 15;119(Pt 4):615-23
ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.
Maattanen P, Kozlov G, Gehring K, Thomas DY
Biochemistry and cell biology = Biochimie et biologie cellulaire 2006 Dec;84(6):881-9
Biochemistry and cell biology = Biochimie et biologie cellulaire 2006 Dec;84(6):881-9
ERp57 binds competitively to protein disulfide isomerase and calreticulin.
Kimura T, Imaishi K, Hagiwara Y, Horibe T, Hayano T, Takahashi N, Urade R, Kato K, Kikuchi M
Biochemical and biophysical research communications 2005 May 27;331(1):224-30
Biochemical and biophysical research communications 2005 May 27;331(1):224-30
Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors.
Chen G, Gharib TG, Huang CC, Thomas DG, Shedden KA, Taylor JM, Kardia SL, Misek DE, Giordano TJ, Iannettoni MD, Orringer MB, Hanash SM, Beer DG
Clinical cancer research : an official journal of the American Association for Cancer Research 2002 Jul;8(7):2298-305
Clinical cancer research : an official journal of the American Association for Cancer Research 2002 Jul;8(7):2298-305
Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading.
Tan P, Kropshofer H, Mandelboim O, Bulbuc N, Hämmerling GJ, Momburg F
Journal of immunology (Baltimore, Md. : 1950) 2002 Feb 15;168(4):1950-60
Journal of immunology (Baltimore, Md. : 1950) 2002 Feb 15;168(4):1950-60
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
Oliver JD, Roderick HL, Llewellyn DH, High S
Molecular biology of the cell 1999 Aug;10(8):2573-82
Molecular biology of the cell 1999 Aug;10(8):2573-82
ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.
Oliver JD, Roderick HL, Llewellyn DH, High S
Molecular biology of the cell 1999 Aug;10(8):2573-82
Molecular biology of the cell 1999 Aug;10(8):2573-82
Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins.
Oliver JD, van der Wal FJ, Bulleid NJ, High S
Science (New York, N.Y.) 1997 Jan 3;275(5296):86-8
Science (New York, N.Y.) 1997 Jan 3;275(5296):86-8
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