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CALR

GeneName

CALR

Summary

CALR, also known as calreticulin or Crt, is a 48 kDa multifunctional protein predominantly located in the endoplasmic reticulum, but also found in various cellular compartments including the cytoplasm, cell surface, and extracellular space. It plays a crucial role in calcium ion homeostasis, protein folding, and quality control within the endoplasmic reticulum. CALR is involved in several biological processes such as cardiac muscle cell differentiation, cellular responses to stimuli, and the regulation of gene expression. It also participates in immune responses by aiding in peptide antigen assembly with MHC class I molecules, and is implicated in processes like phagocytosis and cell migration.

Importance

CALR is relevant to: - Immune regulation and antigen presentation due to its role in MHC class I peptide loading - Cardiovascular research through its involvement in cardiac muscle cell differentiation - Cancer biology as it is associated with cellular responses to stress and apoptosis - Neurobiology, particularly in the context of neuronal differentiation and synaptic function - Disorders related to protein misfolding and endoplasmic reticulum stress, highlighting its role in protein quality control

Top Products

For researchers investigating CALR, we recommend two excellent primary antibodies that cater to a variety of applications. The first is the well-cited polyclonal antibody, Anti-Calreticulin antibody - ER Marker (ab2907), which has garnered 292 citations, highlighting its reliability in Western blotting (WB) and immunocytochemistry (ICC). In addition, we offer the recombinant antibody, Anti-Calreticulin antibody [EPR3924] - ER Marker (ab92516). This product is validated in knockout models and is suitable for a broader range of applications, including WB, ICC, flow cytometry (FC), and immunohistochemistry (IHC). With 173 citations, it demonstrates a solid presence in the research community. The recombinant nature of this antibody ensures batch-to-batch consistency, making it an excellent choice for researchers seeking dependable CALR detection.

Abcam Product Citation Summary

The data indicates a significant focus on the use of CALR antibodies in various human cell lines and models, particularly in the context of cancer research, including studies on acute lung injury, hepatic cells, and breast cancer. The applications primarily involve Western blotting, with some instances of immunocytochemistry and flow cytometry, highlighting the versatility of CALR as a target in different experimental setups.

Abcam Product Citation Table

Product Code
Species
Application
Study Context
PMID
ab223614
Mouse
WB
LPS-induced acute lung injury
32082309
ab22683
Human
WB
Human cell lines
26307067
ab22683
Human
WB
Human hepatic cells and HCC cells
26307067
ab22683
Human
WB
Unfolded protein response
28763460
ab22683
Human
WB
MV4-11 cells and AKT signaling
29285262
ab22683
Human
WB
AML patient samples
29285262
ab2907
Human
WB
HCT116 cells and miR-27a silencing
26913599
ab2907
Human
ICC-IF
RPMI-8226 and SK-MEL-5 cells
30087439
ab2907
Human
ICC
Erythroblasts
32411010
ab2907
Human
WB
Red cell membranes and reticulocyte maturation
32411010
ab2907
Human
FC
Colorectal cancer cells
32046105
ab2907
Human
WB
HCT116 cells and mitoxantrone-induced immunogenic cell death
26913599
ab2907
Human
FC
Lymphoblasts treated with ICD-inducers
31192123
ab2907
Human
ICC-IF
Human cells and conserved interactome of MANF
33460650
ab2907
Mouse
FC
Fibrosarcoma MCA205 cells and immunogenic cell death
32323922
ab2907
Mouse
FC
House mouse cells and cancer cell treatment responses
32323922
ab2907
Human
WB
Breast cancer cells and immunogenic cell death induced by boiling histotripsy
31227775
ab92516
Human
ICC-IF
NPC1 fibroblasts and lysosomal characteristics
32457374
ab92516
Human
WB
NPC CNE2 cells and epithelial-mesenchymal transition
31956372

Domain

Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.

The interaction with glycans occurs through a binding site in the globular lectin domain.

The zinc binding sites are localized to the N-domain.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

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).

Involvement in disease

CALR 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.

Sequence Similarities

Belongs to the calreticulin family.

Cellular localization

Alternative names

CRTC, CALR, Calreticulin, CRP55, Calregulin, Endoplasmic reticulum resident protein 60, HACBP, grp60, ERp60

swissprot:P27797 omim:109091 entrezGene:811