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CALR Matched Antibody Pair (173) (APMAB-173LY)

This antibody pair set can be used for detecting and quantifying protein level of human CALR.
See all CALR antibodies

Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Mouse anti-CALR monoclonal, IgG1 antibody, 100 ug
Detection Antibody
Anti-CALR Rabbit polyclonal antibody, 50 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
Calreticulin is a multifunctional protein that acts as a major Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. It is also found in the nucleus, suggesting that it may have a role in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is almost identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. Calreticulin binds to antibodies in certain sera of systemic lupus and Sjogren patients which contain anti-Ro/SSA antibodies, it is highly conserved among species, and it is located in the endoplasmic and sarcoplasmic reticulum where it may bind calcium. The amino terminus of calreticulin interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. Calreticulin can inhibit the binding of androgen receptor to its hormone-responsive DNA element and can inhibit androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Thus, calreticulin can act as an important modulator of the regulation of gene transcription by nuclear hormone receptors. Systemic lupus erythematosus is associated with increased autoantibody titers against calreticulin but calreticulin is not a Ro/SS-A antigen. Earlier papers referred to calreticulin as an Ro/SS-A antigen but this was later disproven. Increased autoantibody titer against human calreticulin is found in infants with complete congenital heart block of both the IgG and IgM classes. [provided by RefSeq, Jul 2008]
Alternative Names
Calreticulin; Sicca Syndrome Antigen A (Autoantigen Ro; Calreticulin); Endoplasmic Reticulum Resident Protein 60; Calregulin; CRP55; ERp60; HACBP; Grp60; Epididymis Secretory Sperm Binding Protein Li 99n;
Entrez Gene ID
811
UniProt ID
P27797

Fucikova, J., Spisek, R., Kroemer, G., & Galluzzi, L. (2021). Calreticulin and cancer. Cell research, 31(1), 5-16.

Biwer, L. A., Askew-Page, H. R., Hong, K., Milstein, J., Johnstone, S. R., Macal, E., ... & Isakson, B. E. (2020). Endothelial calreticulin deletion impairs endothelial function in aged mice. American Journal of Physiology-Heart and Circulatory Physiology, 318(5), H1041-H1048.

Masubuchi, N., Araki, M., Yang, Y., Hayashi, E., Imai, M., Edahiro, Y., ... & Komatsu, N. (2020). Mutant calreticulin interacts with MPL in the secretion pathway for activation on the cell surface. Leukemia, 34(2), 499-509.

Liu, P., Zhao, L., Loos, F., Marty, C., Xie, W., Martins, I., ... & Kroemer, G. (2020). Immunosuppression by mutated calreticulin released from malignant cells. Molecular cell, 77(4), 748-760.

Araki, M., Yang, Y., Imai, M., Mizukami, Y., Kihara, Y., Sunami, Y., ... & Komatsu, N. (2019). Homomultimerization of mutant calreticulin is a prerequisite for MPL binding and activation. Leukemia, 33(1), 122-131.

Salati, S., Genovese, E., Carretta, C., Zini, R., Bartalucci, N., Prudente, Z., ... & Manfredini, R. (2019). Calreticulin Ins5 and Del52 mutations impair unfolded protein and oxidative stress responses in K562 cells expressing CALR mutants. Scientific reports, 9(1), 1-14.

Bozkus, C. C., Roudko, V., Finnigan, J. P., Mascarenhas, J., Hoffman, R., Iancu-Rubin, C., & Bhardwaj, N. (2019). Immune checkpoint blockade enhances shared neoantigen-induced T-cell immunity directed against mutated calreticulin in myeloproliferative neoplasms. Cancer discovery, 9(9), 1192-1207.

Elf, S., Abdelfattah, N. S., Baral, A. J., Beeson, D., Rivera, J. F., Ko, A., ... & Mullally, A. (2018). Defining the requirements for the pathogenic interaction between mutant calreticulin and MPL in MPN. Blood, The Journal of the American Society of Hematology, 131(7), 782-786.

Biwer, L. A., Good, M. E., Hong, K., Patel, R. K., Agrawal, N., Looft-Wilson, R., ... & Isakson, B. E. (2018). Non–Endoplasmic Reticulum–Based Calr (Calreticulin) Can Coordinate Heterocellular Calcium Signaling and Vascular Function. Arteriosclerosis, thrombosis, and vascular biology, 38(1), 120-130.

Holmström, M. O., Martinenaite, E., Ahmad, S. M., Met, Ö., Friese, C., Kjaer, L., ... & Andersen, M. H. (2018). The calreticulin (CALR) exon 9 mutations are promising targets for cancer immune therapy. Leukemia, 32(2), 429-437.

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For research use only. Not intended for any clinical use.

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