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these data support the model that CALR-mutated essential thrombocythemia could be considered as a distinct disease entity from JAK2V617F-positive myeloproliferative neoplasms
This phenotypic diversity is further emphasized by the following report of a patient with an isolated erythrocytosis, persistent for nearly twelve years, associated with a CALR exon 9 mutation
CALR exon 9 mutation is associated with myeloproliferative neoplasms.
Absence of CALR mutations in JAK2 (zeige JAK2 Proteine)-negative polycythemia.
In 136 patients with myelofibrosis and a median age of 58 years who underwent allogeneic stem cell transplantation (AHSCT) for molecular residual disease, the percentage of molecular clearance on day 100 was higher in CALR-mutated patients (92%) in comparison with MPL (zeige MPL Proteine)- (75%) and JAKV617F-mutated patients (67%).
Mutational subtypes of CALR correlate with different clinical features in Japanese patients with myeloproliferative neoplasms.
CALR mutations is associated with non-hepatosplenic extramedullary hematopoiesis(NHS-EMH) and may possibly contribute to the pathogenesis of primary myelofibrosis -associated NHS-EMH.
This study demonstrated that two patients had a heterozygous CALR exon9 mutation locating outside the coding region and did not alter the amino acid sequence of this protein.
Multivariate analysis adjusted for age, sex, follow-up period and hematological parameters confirmed that increased activated B cells were universally present in JAK2 (zeige JAK2 Proteine)-mutated, CALR-mutated and triple-negative ET patients when compared to healthy adults.
these results reveal proteome alterations in MPN (zeige PRSS27 Proteine) granulocytes depending on the phenotype and genotype of patients, highlighting new oncogenic mechanisms associated with JAK2 (zeige JAK2 Proteine) mutations and overexpression of calreticulin
Calreticulin is required for TGF-beta (zeige TGFB1 Proteine) mediated epithelial-mesenchymal transition and cardiomyogenesis from mESCs.
CALR mutation analysis can thus be a useful additional diagnostic tool to achieve an accurate diagnosis for patients with ET who lack JAK2V617F and MPLW515 mutations
CRT (zeige SLC6A8 Proteine) inhibition significantly blunted APN's anti-oxidative action (evidenced by gp91(phox (zeige CYBB Proteine)) expression and superoxide generation). However, CRT (zeige SLC6A8 Proteine) inhibition did not attenuate AMPK (zeige PRKAA1 Proteine) phosphorylation by APN (zeige ANPEP Proteine) administration in NCM (zeige CWC22 Proteine). Therefore, these novel findings strongly indicate that APN (zeige ANPEP Proteine) exerts cardioprotective effects against I/R injury partially via CRT (zeige SLC6A8 Proteine) mediated anti-apoptotic and anti-oxidative actions.
we show that the homologous mouse CALR del52, ins5 and del61 mutants also activate thrombopoietin receptor (zeige MPL Proteine) signaling via JAK (zeige JAK3 Proteine)-STAT (zeige STAT1 Proteine) pathway
study provides a model showing that the C-terminal of mutant CALR activated JAK (zeige JAK3 Proteine)-STAT (zeige STAT1 Proteine) signaling specifically downstream of MPL (zeige MPL Proteine) and may have a central role in CALR-induced myeloproliferative neoplasms
the results of this investigation provide the first molecular insights into the phospholipid binding site of calreticulin as a key anchor point for the cell surface expression of calreticulin on apoptotic cells
a profound impairment in calreticulin function when its lectin site was inactivated. Remarkably, inactivation of the polypeptide binding site had little impact. These findings indicate that the lectin-based mode of client interaction is the predominant contributor to the chaperone functions of calreticulin within the endoplasmic reticulum.
This essential role of calreticulin in nucleocytoplasmic communication competency ties its regulatory action with proficiency of cardiac myofibrillogenesis essential for proper cardiac development.
Study provides evidence that chronic stress activates calreticulin and might be one of the pathological mechanisms underlying the motor coordination and motor learning dysfunctions seen in social defeat mice.
This study for the first time revealed that increased CRT (zeige SLC6A8 Proteine) inhibited Fas (zeige FAS Proteine)/FasL (zeige FASL Proteine)-mediated neuronal cell apoptosis during the early stage of ischemic stroke, suggesting it to be a potential protector activated soon after ischemia-reperfusion injury
Calreticulin plays a key role in olfactory system function, possibly by establishing its overall sensitivity to odorants.
Calreticulin mediates hypersensitivity to diethylether and resistance to isoflurane in association with low expression of the gene.
These results collectively indicate that calreticulin is the first molecule to be identified as a marker for phagocytosis of apoptotic cells by Drosophila phagocytes
Here the authors identify porcine calreticulin expressed by swine intestinal cells as a host-specific receptor for Salmonella Choleraesuis FimH adhesin, suggesting that such an interaction may contribute to Salmonella Choleraesuis host specificity.
Calreticulin is confined to subplasmalemmal vesicles partially overlapping with cortical granule contents. Its exocytosis after the oocyte activation seems to participate in the membrane block to polyspermy in pigs.
Calreticulin was widely expressed in pig tissues and its transcripts were downregulated during maturation, especially at 44 hr, and were undetectable at the blastocyst stage.
the lectin site of CRT is the main target for gentamicin binding
These findings suggest that protein kinase C is involved in the regulation of CRT function.
Nkx2.5 signaling via activation of Nkx2.5-Calr-p53 (zeige TP53 Proteine) signaling pathway results in cardiac dysfunction and hyperglycemia-induced cardiomyopathy.
These findings showed that mutant CALR activates jak (zeige JAK3 Proteine)-stat (zeige STAT1 Proteine) signaling through an mpl (zeige MPL Proteine)-dependent mechanism to mediate pathogenic thrombopoiesis in zebrafish, and illustrated that the signaling machinery related to mutant CALR tumorigenesis are conserved between human and zebrafish.
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.
, Sicca syndrome antigen A (autoantigen Ro; calreticulin)
, endoplasmic reticulum resident protein 60
, pot pourri
, calcium-binding protein 3
, Endoplasmic reticulum resident protein 60
, calreticulin, like 2