PDIA3 antibody (Protein Disulfide Isomerase Family A, Member 3)

Details for Product anti-PDIA3 Antibody No. ABIN361814, Supplier: Log in to see
Antigen
  • 58kDa
  • ERp57
  • ERp60
  • ERp61
  • Erp
  • Grp58
  • PDI
  • PDI-Q2
  • PI-PLC
  • PLC[a]
  • Plca
  • ER60
  • GRP57
  • GRP58
  • HsT17083
  • P58
  • grp-58
  • 1
  • 25D3-membrane-associated
  • zgc:100906
  • protein disulfide-isomerase A3
  • protein disulfide isomerase family A, member 3
  • protein disulfide isomerase associated 3
  • zgc:100906
  • Tsp_10062
  • PDIA3
  • Pdia3
Alternatives
anti-Cow (Bovine) PDIA3 antibody for Immunofluorescence
Reactivity
Cow (Bovine), Dog (Canine), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus)
233
103
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72
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70
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67
10
8
8
4
4
4
4
4
3
3
2
Host
Mouse
122
92
22
Clonality (Clone)
Monoclonal ()
Conjugate
This PDIA3 antibody is un-conjugated
12
11
9
4
4
4
3
3
3
3
3
3
3
3
3
3
2
2
2
2
2
2
2
2
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2
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
218
100
94
78
55
49
35
15
5
2
2
2
1
Options
Supplier
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Supplier Product No.
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Immunogen Human recombinant ERp57 (Grp58)
Clone Map-ERp57
Isotype IgG1
Specificity Detects ~57 kDa.
Purification Protein G Purified
Alternative Name ERp57 (PDIA3 Antibody Abstract)
Background ERp57, also known as Glucose Regulated Protein 58 (Grp58), Hormone-Induced Protein-70 (HIP-70) and microsomal Carnitine Palmitoyltransferase, is a member of the protein disulfide isomerase family, containing two canonical CXHC tetrapeptide active site motifs (1-5). It has quite a few diverse roles. It functions as an accessory oxidoreductase involved in disulfide bond formation. In the ER, ERp57 interacts with membrane bound calnexin and soluble calreticulin (lectin chaperones) via their praline rich P-domain arms. Lectin chaperones bind nascent non-native glycoproteins, and position ERp57 to act upon the immature or misfolded glycoproteins that possess mono-glycosylated side chains. ERp57 deletion impairs posttranslational phases of influenza hema-glutinin folding, and causes accelerated release of MHC-I molecules, resulting in the coupling of sub-optimal peptides and reduced expression and stability on the cell surface (6). ERp57 also contains two thioredoxin active-site sequences, CGHC and an estrogen-binding domain. ERp57 is induced by both estrogen and leuteinizing-hormone-releasing hormone in the hippocampus (7).
Gene ID 2923
NCBI Accession NP_005304
UniProt P30101
Research Area Signaling
Pathways Maintenance of Protein Location, Protein targeting to Nucleus, Cell RedoxHomeostasis
Application Notes
  • WB (1:2000)
  • IHC (1:100)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

0.5 μg/ml of SMC-168 was sufficient for detection of ERp57 in 10 μg of heat shock Heal Lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-Protein Disulfide Isomerase Family A, Member 3 (PDIA3) antibody (ABIN361814) Erp57 Western Blotting 1 in 1000 Hu copy.
Product cited in: Ortiz-Sandoval, Hughes, Dacks, Simmen: "Interaction with the effector dynamin-related protein 1 (Drp1) is an ancient function of Rab32 subfamily proteins." in: Cellular logistics, Vol. 4, Issue 4, pp. e986399, 2015 (PubMed).

Lynes, Raturi, Shenkman, Ortiz Sandoval, Yap, Wu, Janowicz, Myhill, Benson, Campbell, Berthiaume, Lederkremer, Simmen: "Palmitoylation is the switch that assigns calnexin to quality control or ER Ca2+ signaling." in: Journal of cell science, Vol. 126, Issue Pt 17, pp. 3893-903, 2013 (PubMed).

Background publications Leclercq, Lardet, Martin, Chapuset, Oliver, Montoro: "The green fluorescent protein as an efficient selection marker for Agrobacterium tumefaciens-mediated transformation in Hevea brasiliensis (Müll. Arg)." in: Plant cell reports, Vol. 29, Issue 5, pp. 513-22, 2010 (PubMed).

Hebert, Molinari: "In and out of the ER: protein folding, quality control, degradation, and related human diseases." in: Physiological reviews, Vol. 87, Issue 4, pp. 1377-408, 2007 (PubMed).

Maattanen, Kozlov, Gehring, Thomas: "ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations." in: Biochemistry and cell biology = Biochimie et biologie cellulaire, Vol. 84, Issue 6, pp. 881-9, 2007 (PubMed).

Soldà, Garbi, Hämmerling, Molinari: "Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle." in: The Journal of biological chemistry, Vol. 281, Issue 10, pp. 6219-26, 2006 (PubMed).

Williams: "Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum." in: Journal of cell science, Vol. 119, Issue Pt 4, pp. 615-23, 2006 (PubMed).

Kimura, Imaishi, Hagiwara, Horibe, Hayano, Takahashi, Urade, Kato, Kikuchi: "ERp57 binds competitively to protein disulfide isomerase and calreticulin." in: Biochemical and biophysical research communications, Vol. 331, Issue 1, pp. 224-30, 2005 (PubMed).

Chen, Gharib, Huang, Thomas, Shedden, Taylor, Kardia, Misek, Giordano, Iannettoni, Orringer, Hanash, Beer: "Proteomic analysis of lung adenocarcinoma: identification of a highly expressed set of proteins in tumors." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 8, Issue 7, pp. 2298-305, 2002 (PubMed).

Tan, Kropshofer, Mandelboim, Bulbuc, Hämmerling, Momburg: "Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 168, Issue 4, pp. 1950-60, 2002 (PubMed).

Oliver, Roderick, Llewellyn, High: "ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin." in: Molecular biology of the cell, Vol. 10, Issue 8, pp. 2573-82, 1999 (PubMed).

Oliver, van der Wal, Bulleid, High: "Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins." in: Science (New York, N.Y.), Vol. 275, Issue 5296, pp. 86-8, 1997 (PubMed).

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