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Purified Mouse Anti-Calreticulin
Purified Mouse Anti-Calreticulin

Western blot analysis of calreticulin on a mouse testis lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10000 dilution of the anti- calreticulin antibody.

Purified Mouse Anti-Calreticulin

Immunoflourescence staining of the human lung cell line, WI38.

Western blot analysis of calreticulin on a mouse testis lysate. Lane 1: 1:2500, lane 2: 1:5000, lane 3: 1:10000 dilution of the anti- calreticulin antibody.

Immunoflourescence staining of the human lung cell line, WI38.

Product Details
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BD Transduction Laboratories™
Mouse (QC Testing), Human, Rat (Tested in Development)
Mouse IgG1
Mouse Calreticulin aa. 270-390
Western blot (Routinely Tested), Immunofluorescence (Tested During Development)
60 kDa
250 µg/ml
AB_399508
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Preparation And Storage

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

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to www.bdbiosciences.com/us/s/resources 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.
612137 Rev. 1
Antibody Details
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16/Calreticulin

Proteins undergo numerous modifications, including folding, translocation, and degradation. During such modifications, polypeptides are rarely in a native, stable state. Molecular chaperones are a diverse group of proteins that modulate polypeptide stability through ATP-dependent folding. Many chaperone proteins are found in the endoplasmic reticulum (ER). Calreticulin is a luminal ER protein that is 39% homologous to the ER chaperone protein, calnexin. Calreticulin contains a C-terminal KDEL ER retention signal, and can bind Ca2+, Zn2+, ATP, and the proteins, ERp57 and protein disulfide isomerase. The molecular chaperone activities of calreticulin may include folding of both Asn-linked glycoproteins and non-glycosylated proteins. In addition, calreticulin is a component of MHC I/transporter associated with Ag presentation (TAP) complex where it may function in peptide assembly onto nascent class I molecules. Calreticulin may also function in integrin signaling, since it binds a3-integrin subunits and regulates integrin-mediated metalloprotease secretion. Thus, calreticulin may be involved in Ca2+ storage, cell adhesion, and protein folding.

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.

612137 Rev. 1
Format Details
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Purified
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.
Purified
612137 Rev.1
Citations & References
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Development References (4)

  1. Ito H, Seyama Y, Kubota S. Calreticulin is directly involved in anti-alpha3 integrin antibody-mediated secretion and activation of matrix metalloprotease-2. Biochem Biophys Res Commun. 2001; 283(2):297-302. (Biology). View Reference
  2. Mazzarella RA, Gold P, Cunningham M, Green M. Determination of the sequence of an expressible cDNA clone encoding ERp60/calregulin by the use of a novel nested set method. Gene. 1992; 120(2):217-225. (Biology). View Reference
  3. Nair S, Wearsch PA, Mitchell DA, Wassenberg JJ, Gilboa E, Nicchitta CV. Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. J Immunol. 1999; 162(11):6426-6432. (Biology). View Reference
  4. Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J. 1999; 18(23):6718-6729. (Biology). View Reference
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612137 Rev. 1

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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.