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Merck
CN

C4606

Anti-Calreticulin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
immunoprecipitation (IP)
indirect immunofluorescence
microarray
western blot
Species reactivity:
human, canine
Citations:
25
Technique(s):
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 accession no.:
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Product Name

Anti-Calreticulin antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 50 kDa

species reactivity

human, canine

technique(s)

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 accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... CALR(811)

Application

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

Biochem/physiol Actions

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

Disclaimer

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.

General description

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.

Immunogen

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

Physical form

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

Preparation Note

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.

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Storage Class

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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N Limsuwanachot et al.
Hematology (Amsterdam, Netherlands), 22(10), 599-606 (2017-04-14)
Classical BCR-ABL1-negative myeloproliferative neoplasms (MPNs) including polycythemia vera, essential thrombocythemia (ET), and primary myelofibrosis frequently harbor JAK2, MPL, and CALR somatic mutations. AS-PCR for JAK2 V617F, pyrosequencing for MPL W515L/K, and PCR-fragment analysis for CALR exon 9 mutations were established
Marek Michalak et al.
The Biochemical journal, 417(3), 651-666 (2009-01-13)
Calreticulin is an ER (endoplasmic reticulum) luminal Ca2+-buffering chaperone. The protein is involved in regulation of intracellular Ca2+ homoeostasis and ER Ca2+ capacity. The protein impacts on store-operated Ca2+ influx and influences Ca2+-dependent transcriptional pathways during embryonic development. Calreticulin is
Eleonora Di Gregorio et al.
American journal of human genetics, 95(2), 209-217 (2014-07-30)
Spinocerebellar ataxias (SCAs) are a heterogeneous group of autosomal-dominant neurodegenerative disorders involving the cerebellum and 23 different genes. We mapped SCA38 to a 56 Mb region on chromosome 6p in a SCA-affected Italian family by whole-genome linkage analysis. Targeted resequencing
Pascal Gelebart et al.
The international journal of biochemistry & cell biology, 37(2), 260-266 (2004-10-12)
Calreticulin is a 46-kDa Ca2+-binding chaperone found across a diverse range of species. The protein is involved in the regulation of intracellular Ca2+ homeostasis and endoplasmic reticulum (ER) Ca2+ storage capacity. Calreticulin is also an important molecular chaperone involved in
Alexander Domnick et al.
Nature communications, 13(1), 4701-4701 (2022-08-11)
Major histocompatibility complex class I (MHC I) molecules are central to adaptive immunity. Their assembly, epitope selection, and antigen presentation are controlled by the MHC I glycan through a sophisticated network of chaperones and modifying enzymes. However, the mechanistic integration

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