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Protein Disulfide Isomerase Family A, Member 4 (PDIA4) (AA 427-642) antibody

Details for Product No. ABIN968286
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Antigen
Synonyms LOC100229535, cai, wu:fd20c07, zgc:113965, zgc:136625, zgc:56014, zgc:77773, AI987846, Cai, ERp-72, Erp72, ERP70, ERP72, Erp70
Epitope
AA 427-642
(11), (7), (4), (2), (2), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(53), (22), (19), (14), (4), (3), (2), (1), (1), (1), (1)
Host
Mouse
(38), (20)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), Immunofluorescence (IF)
(49), (16), (12), (10), (9), (8), (4), (1), (1)
Pubmed 4 references available
Quantity 50 µg
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Catalog No. ABIN968286
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Immunogen Human ERp72
Clone 3
Isotype IgG1
Cross-Reactivity Rat (Rattus)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name ERp72
Background Within the ER lumen, numerous molecular chaperones transiently bind nascent proteins and facilitate their folding or assembly. The action of chaperones ensures proper folding and, in turn, transport of new proteins from the rough ER to the Golgi complex. Some chaperones (grp78/Bip) bind to exposed hydrophobic segments, while others (ERp59/PDI) are involved in disulfide isomerization. An ERp59/PDI related protein, ERp72, contains three copies of the PDI acitve site, CGHC. Although ERp72 participates in disulfide isomerization, it is unclear whether it functions alone or in conjunction with other chaperones, specifically other members of the CGHC-containing protein family. Many chaperones, including PDI, are held within the ER via the common C-terminal KDEL sequence. ERp72 contains a related KEEL sequence that is essential for its ER retention. Additional studies have shown that ERp72 is a protease and a member of the thioredoxin superfamily known to bind Ca2+. Thus, ERp72 functions as a Ca2+-dependent chaperone with disulfide isomerization activity, but also may undertake other, yet undefined, roles within the ER. This antibody is routinely tested by western blot analysis.
Molecular Weight 69 kDa
Research Area Signaling
Comment

Related Products: ABIN967389, ABIN968537

Restrictions For Research Use only
Format Liquid
Concentration 250 µg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
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
anti-Protein Disulfide Isomerase Family A, Member 4 (PDIA4) (AA 427-642) antibody Western blot analysis of ERp72 on a Jurkat cell lysate (Human T-cell leukemia, ATCC TIB-152). Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the mouse anti-ERp72 antibody.
anti-Protein Disulfide Isomerase Family A, Member 4 (PDIA4) (AA 427-642) antibody (2) Immunofluorescence staining of human endothelial cells.
anti-Protein Disulfide Isomerase Family A, Member 4 (PDIA4) (AA 427-642) antibody (3) anti-Protein Disulfide Isomerase Family A, Member 4 (PDIA4) (AA 427-642) antibody (Image 3)
Product cited in: Mazzarella, Srinivasan, Haugejorden et al.: "ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase." in: The Journal of biological chemistry, Vol. 265, Issue 2, pp. 1094-101, 1990 (PubMed).

Kuznetsov, Chen, Nigam: "Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation." in: The Journal of biological chemistry, Vol. 269, Issue 37, pp. 22990-5, 1994 (PubMed).

Nigam, Goldberg, Ho et al.: "A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily." in: The Journal of biological chemistry, Vol. 269, Issue 3, pp. 1744-9, 1994 (PubMed).

Daoudal, Tournaire, Halere et al.: "Isolation of the mouse aldose reductase promoter and identification of a tonicity-responsive element." in: The Journal of biological chemistry, Vol. 272, Issue 5, pp. 2615-9, 1997 (PubMed).

Validation Images
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