CALR Antibody - #DF6211
*The optimal dilutions should be determined by the end user.
Cite Format: Affinity Biosciences Cat# DF6211, RRID:AB_2838177.
Autoantigen RO; CALR; CALR protein; CALR_HUMAN; Calregulin; Calreticulin; cC1qR; CRP55; CRT; CRTC; Endoplasmic reticulum resident protein 60; Epididymis secretory sperm binding protein Li 99n; ERp60; FLJ26680; grp60; HACBP; HEL S 99n; RO; Sicca syndrome antigen A (autoantigen Ro; calreticulin); Sicca syndrome antigen A; SSA;
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P27797 As Substrate
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. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).
Endoplasmic reticulum lumen. Cytoplasm>Cytosol. Secreted>Extracellular space>Extracellular matrix. Cell surface. Sarcoplasmic reticulum lumen.
Note: Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). Associated with the lytic granules in the cytolytic T-lymphocytes.
Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and SPACA9 (By similarity). Interacts with TRIM21. Interacts with NR3C1. Interacts with PPIB. Interacts (via P-domain) with PDIA5. Interacts with GABARAP. Interacts with HLA-E-B2M and HLA-G-B2M complexes. Interacts with HLA-F. Interacts with CLCC1.
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.
Belongs to the calreticulin family.
· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).
· Human Diseases > Infectious diseases: Viral > HTLV-I infection.
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