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Purified Mouse Anti-ERp72
Purified Mouse Anti-ERp72

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.

Purified Mouse Anti-ERp72

Immunofluorescence staining of human endothelial cells.

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.

Immunofluorescence staining of human endothelial cells.

Product Details
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BD Transduction Laboratories™
Human (QC Testing), Rat (Tested in Development)
Mouse IgG1
Human ERp72 aa. 427-642
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
69 kDa
250 µg/ml
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at -20°C.

Recommended Assay Procedures

Western blot:  Please refer to

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to 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.
610970 Rev. 1
Antibody Details
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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. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.

610970 Rev. 1
Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
610970 Rev.1
Citations & References
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Development References (4)

  1. Daoudal S, Tournaire C, Halere A, Veyssiere G, Jean C. Isolation of the mouse aldose reductase promoter and identification of a tonicity-responsive element. J Biol Chem. 1997; 272(5):2615-2619. (Biology). View Reference
  2. Kuznetsov G, Chen LB, Nigam SK. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J Biol Chem. 1994; 269(37):22990-22995. (Biology). View Reference
  3. Mazzarella RA, Srinivasan M, Haugejorden SM, Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem. 1990; 265(2):1094-1101. (Biology). View Reference
  4. Nigam SK, Goldberg AL, Ho S, Rohde MF, Bush KT, Sherman MYu. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. J Biol Chem. 1994; 269(3):1744-1749. (Biology). View Reference
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610970 Rev. 1

Please refer to Support Documents for Quality Certificates

Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described

Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.