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C7492

Sigma-Aldrich

Monoclonal Anti-Calreticulin antibody produced in mouse

clone TO-11, tissue culture supernatant, buffered aqueous solution

Synonym(s):

Calreticulin Antibody Flow Cytometry, Anti-Autoantigen Ro

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.44

biological source

mouse

conjugate

unconjugated

antibody form

tissue culture supernatant

antibody product type

primary antibodies

clone

TO-11, monoclonal

form

buffered aqueous solution

mol wt

antigen ~50 kDa

species reactivity

human

technique(s)

flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: 1:50-1:100 using total cell extract of HeLa cells

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... CALR(811)

General description

Monoclonal Anti-Calreticulin (mouse IgG1 isotype) is derived from the hybridoma TO-11 produced by the fusion of mouse myeloma cells (P3-X63-AG8.653 cells) and splenocytes from BALB/c mice.
Monoclonal Anti-Calreticulin (mouse IgG1 isotype) is derived from the hybridoma TO-11 produced by the fusion of mouse myeloma cells (P3-X63-AG8.653 cells) and splenocytes from BALB/c mice. Calreticulin is a molecular chaperones in endoplasmic reticulum lumen. Calreticulin acts as a lectin-like chaperone binding oligosaccharide residues of newly synthesized N-linked glycoproteins, and misfolded proteins. Calreticulin is a protein binding Ca2+ ions. It is encoded by the CALR gene in humans.

Application

Monoclonal Anti-Calreticulin antibody produced in mouse is suitable for the following applications:
  • Flow cytometry
  • Immunocytochemistry
  • Immunohistochemistry
  • Indirect ELISA
  • Western blotting

Biochem/physiol Actions

Calreticulin and Its variants causes differential effects on thrombopoiesis. Somatic mutations of calreticulin (CALR) gene causes thrombocythemia (ET) and primary myelofibrosis (PMF).
It is believed to play a critical role in quality control processes during protein synthesis and folding. Increased expression of calreticulin increases 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+ -ATPase (SERCA). Overexpression of calreticulin results in increased sensitivity of HeLa cells to drug-induced apoptosis. In contrast, calreticulin-deficient cells show increased resistance to apoptosis. Calreticulin gene disruption leads toimpairment of cardiac development. Loss of calreticulin function favors ubiquitin-proteosome activity. It plays a critical role in Ca2+ homeostasis.

Physical form

Culture supernatant solution containing 15 mM sodium azide.

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Ayalew Tefferi et al.
American journal of hematology, 89(8), E121-E124 (2014-04-23)
CALR (calreticulin) trails JAK2 as the second most mutated gene in essential thrombocythemia (ET). Mutant CALR in ET is a result of frameshift mutations, caused by exon 9 deletions or insertions; type-1, 52-bp deletion (p.L367fs*46), and type-2, 5-bp TTGTC insertion
Enhanced ubiquitin-proteasome activity in calreticulin deficient cells: a compensatory mechanism for cell survival
Uvarov AVand Mesaeli N
Biochimica et Biophysica Acta, 1783(6), 1237-1247 (2008)
Calnexin and calreticulin, molecular chaperones of the endoplasmic reticulum
Calreticulin, 49-62 (2003)
Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum
Gelebart P, et al.
The International Journal of Biochemistry & Cell Biology, 37(2), 260-266 (2005)
Functional roles of calreticulin in cancer biology
Lu YC, et al.
BioMed Research International (2015)

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