biological source
rabbit
Quality Level
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
Gene Information
human ... CALR(811)
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).
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.
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.
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.
存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
低风险生物材料
此项目有
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
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
全球贸易项目编号
| 货号 | GTIN |
|---|---|
| C4606-.2ML | 04061838104335 |