Technical Data
Calreticulin (CALR, SSA, Sicca Syndrome Antigen A, Ro, Autoantigen Ro)
Calreticulin is a multifunctional, highly conserved Ca2+ -binding protein that is localized to the endoplasmic reticulum (ER). It is also a molecular chaperone and is involved in protein folding events in the ER. Calreticulin has also been shown to interact with the cytoskeleton and to be involved in the regulation of gene expression. Calreticulin may play a role in cellular proliferation including its apparent activity in the proliferation of certain viruses within mammalian host cells. Recently it has been shown that calreticulin is induced in response to various types of cell stress including amino acid deprivation.
Close interconnections among protein synthesis, gene expression and calcium signaling have been observed by many researchers in recent years. Calreticulin might be centrally located and crucially participate in the coordination of these functions by the cell.

Cellular Localization: Calreticulin staining is localized to the ER in most cell types and under most conditions.

Suitable for use in Western Blot. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot Store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
100ul-20CBlue IceMouseRabbit
Not determined
A full-length protein to mouse calreticulin.
Whole antisera
As reported
This antibody is specific for calreticulin. Species Crossreactivity: Human. Others not tested.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. R. Heal and J. McGivan. Induction of calreticulin expression in response to amino acid deprivation in Chinese hamster ovary cells. Biochemical Journal, 329: 389-394, 1998.
2. K-H Krause and M. Michalak. Calreticulin. Cell. 88: 439-443, 1997.
3. P.D. Nash et al, Calreticulin: not just another calcium-binding protein. Molecular and Cellular Biochemistry, 135: 71-78, 1994.
4. Llewellyn, D.H., et al. Calreticulin comes of age. trends in Cell Biology. 10: 399-402, 2000.