Gene Product Capn3 NM_007601 Calpain 3 S100a3 NM_011310 S100 calcium binding protein A3 Camkk1 NM_018883 Calcium/calmodulin-dependent protein kinase kinase 1 Efcab4a NM_001025103 EF-hand calcium binding domain 4A alpha polypeptide 7 Pcdhb11 NM_053136 Protocadherin beta 11 Calr NM_00759 Calreticulin
Gene Symbol Fold Change p-Value Capn3 +1.
The research also shows that most normal cell populations don't display calreticulin
and are therefore not depleted when we expose them to a blocking anti-CD47 antibody," Weissman said.
A new acetyl CoA independent acetylation of proteins catalyzed by acetoxy drug: calreticulin transacetylase system is also described here and its role in modulating the cellular response similar to that of histone deacetylase (HDAC) inhibitors (Fig.
Recently, existence of a novel enzymatic acetylation system catalyzed by calreticulin an endoplasmic reticulum(ER) resident protein, has been reported, that acetylates target protein by using polyphenolic acetates as the acetyl group donor molecule.
Induction of calreticulin
expression in response to amino acid deprivation in Chinese hamster ovary cells.
The rheumatoid arthritis shared epitope triggers innate immune signaling via cell surface calreticulin
Malignant tumors exhibited increases in proliferating cell nuclear antigen, OP18, pHSP60, HSP90, and calreticulin
and decreases in tropomyosin-1 and -2 when compared with benign tumors.
Reliable diagnostic tools under development for mutations of calreticulin
(CALR) are expected to benefit patients with blood disorders known as myeloproliferative neoplasms
Endoplasmic reticulum chaperones GRP78 and calreticulin
prevent oxidative stress, [Ca.
NASDAQ: NEO), a leading provider of cancer-focused genetic testing services, announced today that it has validated and launched a new test for the detection of mutations in the calreticulin
Frequent Mutations in the Calreticulin
Gene CALR in Myeloproliferative Neoplasms[ LBA-1 ]
Cell lysates were depleted of either intact antigen or the main heat shock proteins gp96, HSP90, HSP70 and calreticulin
, which constitute more than 90 percent of the peptide-binding chaperones in cells.