Human Recombinant CALR protein, hFc Tag (V2LY-0526-LY2517)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
hFc Tag
Protein Construction
This product is Human Recombinant CALR protein, hFc Tag consist of Amino Acid: 1-413 and predicts a molecular mass of 73 kDa.
Molecule Mass
73 kDa
Sequence
Amino Acid: 1-413
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Calreticulin
Function
Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246).
Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926).
Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).
Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Biological Process
Antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
Antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
ATF6-mediated unfolded protein response Source: Reactome
Cardiac muscle cell differentiation Source: Ensembl
Cellular calcium ion homeostasis Source: UniProtKB
Cellular response to lithium ion Source: Ensembl
Cellular senescence Source: BHF-UCL
Cortical actin cytoskeleton organization Source: Ensembl
Endoplasmic reticulum unfolded protein response Source: GO_Central
Glucocorticoid receptor signaling pathway Source: BHF-UCL
Negative regulation of cell cycle arrest Source: BHF-UCL
Negative regulation of intracellular steroid hormone receptor signaling pathway Source: BHF-UCL
Negative regulation of neuron differentiation Source: BHF-UCL
Negative regulation of retinoic acid receptor signaling pathway Source: BHF-UCL
Negative regulation of transcription, DNA-templated Source: BHF-UCL
Negative regulation of transcription by RNA polymerase II Source: BHF-UCL
Negative regulation of translation Source: BHF-UCL
Negative regulation of trophoblast cell migration Source: CAFA
Peptide antigen assembly with MHC class I protein complex Source: BHF-UCL
Positive regulation of cell cycle Source: BHF-UCL
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of dendritic cell chemotaxis Source: UniProtKB
Positive regulation of endothelial cell migration Source: CAFA
Positive regulation of gene expression Source: Ensembl
Positive regulation of NIK/NF-kappaB signaling Source: Ensembl
Positive regulation of phagocytosis Source: BHF-UCL
Positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
Protein export from nucleus Source: UniProtKB
Protein folding Source: GO_Central
Protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
Protein localization to nucleus Source: UniProtKB
Protein maturation by protein folding Source: BHF-UCL
Protein stabilization Source: UniProtKB
Receptor-mediated endocytosis Source: Reactome
Regulation of apoptotic process Source: UniProtKB
Regulation of meiotic nuclear division Source: Ensembl
Regulation of transcription, DNA-templated Source: ProtInc
Response to drug Source: Ensembl
Response to estradiol Source: Ensembl
Response to testosterone Source: Ensembl
Sequestering of calcium ion Source: BHF-UCL
Spermatogenesis Source: Ensembl
Vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane Source: Reactome
Cellular Location
Extracellular matrix; Cytolytic granule; Endoplasmic reticulum lumen; Cytosol; Cell surface; Sarcoplasmic reticulum lumen; Cortical granule. Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity).
Involvement in disease
CARL somatic mutations are frequently found in myeloproliferative neoplasms lacking JAK2 or MPL mutations. Myeloproliferative neoplasms are chronic myeloid cancers characterized by overproduction of mature blood cells, and may evolve into acute myeloid leukemia. In addition to chronic myeloid leukemia with the BCR-ABL fusion gene, the three most common myeloproliferative neoplasms are essential thrombocythemia, polycythemia vera, and myelofibrosis.

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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