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Merck

C4606

Sigma-Aldrich

Anti-Calreticulin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.43

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Mol-Gew.

antigen 50 kDa

Speziesreaktivität

human, canine

Methode(n)

immunoprecipitation (IP): suitable using whole cell RIPA lysate of the human epitheloid carcinoma HeLa cell line
indirect immunofluorescence: 1:100 using 3% paraformaldehyde-fixed, 0.5% Triton X-100 treated, Madin Darby canine kidney MDCK cell line
microarray: suitable
western blot: 1:2,000 using whole cell RIPA lysate of the human epitheloid carcinoma HeLa cell line

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... CALR(811)

Allgemeine Beschreibung

The gene for calreticulin (CALR) is located on the human chromosome 19p13.13. The encoded protein is a predominantly conserved calcium-binding chaperone, which is localized primarily to the lumen of the endoplasmic reticulum (ER). Calreticulin comprises three domains, a globular N-domain, a proline-rich P-domain, and a highly acidic C-domain.

Spezifität

Anti-Calreticulin recognizes human and dog calreticulin (55-60 kDa).

Immunogen

synthetic peptide corresponding to the C-terminus of human calreticulin (amino acids 401-417).

Anwendung

Anti-Calreticulin antibody produced in rabbit has been used in:
  • immunoblotting
  • immunofluorescence
  • immunocytochemistry{91
  • immunoprecipitation

Biochem./physiol. Wirkung

Calreticulin facilitates transient interaction with newly synthesized cellular and extracellular proteins for folding and assembling in the endoplasmic reticulum (ER) before its localization to the cytosol or cell surface. Calreticulin acts as a lectin-like chaperone binding oligosaccharide residues of newly synthesized N-linked glycoproteins and misfolded proteins. It is believed to play a critical role in quality control processes during protein synthesis and folding and calcium (Ca2+) homeostasis. Increased expression of calreticulin increases the Ca2+ storage capacity of the ER. It also appears to modulate store-operated Ca2+-influx and to alter Ca2+ transport by the sarcoplasmic/ER Ca2+-adenosine triphosphatase (ATPase) (SERCA). Overexpression of calreticulin results in increased sensitivity of HeLa cells to drug-induced apoptosis. However, increased resistance to apoptosis has been observed in calreticulin-deficient cells.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Lagerung und Haltbarkeit

Store at -20 °C. For continuous use, the product maybe stored at 2-8 °C for up to one month. For prolonged storage, freeze in working aliquots at-20 °C. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded ifnot used within 12 hours.

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

L M John et al.
The Journal of cell biology, 142(4), 963-973 (1998-08-29)
In Xenopus laevis oocytes, overexpression of calreticulin suppresses inositol 1,4,5-trisphosphate-induced Ca2+ oscillations in a manner consistent with inhibition of Ca2+ uptake into the endoplasmic reticulum. Here we report that the alternatively spliced isoforms of the sarcoendoplasmic reticulum Ca2+-ATPase (SERCA)2 gene
S Johnson et al.
Trends in cell biology, 11(3), 122-129 (2001-04-18)
Calreticulin was first isolated 26 years ago. Since its discovery as a minor Ca(2+)-binding protein of the sarcoplasmic reticulum, the appreciation of its importance has grown, and it is now recognized to be a multifunctional protein, most abundant in the
L Mery et al.
The Journal of biological chemistry, 271(16), 9332-9339 (1996-04-19)
The widely distributed and highly conserved Ca(2+)-binding protein calreticulin has been suggested to play a role as a Ca2+ storage protein of intracellular Ca+ stores. To test this hypothesis, we have generated a mouse L fibroblast cell line stably transfected
K Nakamura et al.
The Journal of cell biology, 150(4), 731-740 (2000-08-23)
To test the role of ER luminal environment in apoptosis, we generated HeLa cell lines inducible with respect to calreticulin and calnexin and investigated their sensitivity to drug-dependent apoptosis. Overexpression of calreticulin, an ER luminal protein, resulted in an increased
Y Saito et al.
The EMBO journal, 18(23), 6718-6729 (1999-12-03)
Calreticulin (CRT) is thought to be a molecular chaperone that interacts with glycoproteins exclusively through a lectin site specific for monoglucosylated oligosaccharides. However, this chaperone function has never been directly demonstrated nor is it clear how lectin-oligosaccharide interactions facilitate glycoprotein

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