产品名称
Monoclonal Anti-Calreticulin antibody produced in mouse, clone TO-11, tissue culture supernatant, buffered aqueous solution
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
Quality Level
Gene Information
human ... CALR(811)
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.
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
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.
Physical form
Culture supernatant solution containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Irradiation enhances the therapeutic effect of the oncolytic adenovirus XVir-N-31 in brain tumor initiating cells
Czolk R, et al.
International Journal of Molecular Medicine (2019)
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
Rebecca Czolk et al.
International journal of molecular medicine, 44(4), 1484-1494 (2019-08-23)
Virotherapy using oncolytic viruses is an upcoming therapy strategy for cancer treatment. A variety of preclinical and clinical trials have indicated that adenoviruses may be used as potent agents in the treatment of a variety of cancers, and also for
Elisa Rumi et al.
Blood, 123(15), 2416-2419 (2014-02-21)
Somatic mutations in the calreticulin (CALR) gene were recently discovered in patients with sporadic essential thrombocythemia (ET) and primary myelofibrosis (PMF) lacking JAK2 and MPL mutations. We studied CALR mutation status in familial cases of myeloproliferative neoplasm. In a cohort
Functional roles of calreticulin in cancer biology
Lu YC, et al.
BioMed Research International (2015)
相关内容
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