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one additional protein, namely P58 (show CDK11B Proteins)(IPK), specifically precipitated with Akita proinsulin (show INS Proteins) and approximately ten fold more PDIA6, but not other PDI (show PDIA3 Proteins) family members, was bound to Akita proinsulin (show INS Proteins). The latter suggests that PDIA6 may act as a key reductase
these findings demonstrated that ER Ca2 (show CA2 Proteins)+, PDIA6, IRE1alpha (show ERN1 Proteins), and miR (show MLXIP Proteins)-322 function in a dynamic feedback loop modulating the UPR under conditions of disrupted ER Ca2 (show CA2 Proteins)+ homeostasis.
By facilitating disulfide bond formation, and enhanced ER protein folding, PDIA6 may contribute to the protective effects of ATF6 (show ATF6 Proteins) in the ischemic mouse heart.
Downregulation of PDIA6 inhibited BC cell proliferation and invasion in vitro as well as tumor growth and metastasis in vivo. In addition, PDIA6 downregulation suppressed the Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling pathway.
Results indicate that re-expression of miR (show MLXIP Proteins)-127-3p and miR (show MLXIP Proteins)-376a-3p induces a strong tumor suppressor effect in GCTSC, which is partially mediated via COA1 (show UBXN11 Proteins) and PDIA6.
ACE (show ACE Proteins) and PDIA6 were identified as potential HSPA2 (show HSPA2 Proteins)-interacting proteins; this assemblage resides in membrane raft microdomains located in the peri (show PLIN1 Proteins)-acrosomal region of the sperm head.
Restoration of miR (show MLXIP Proteins)-127-3p and miR (show MLXIP Proteins)-376a-3p counteracts the neoplastic phenotype of giant cell tumor of bone derived stromal cells by targeting COA1 (show UBXN11 Proteins), GLE1 (show GLE1 Proteins) and PDIA6.
PDIA3 (show PDIA3 Proteins) and PDIA6 gene expression is a neoplasm aggressiveness marker in primary ductal breast cancer.
CDDP-resistant non-small lung cancer cells undergo profound remodeling of their endoplasmic reticulum (ER) proteome (>80 proteins identified by proteomics) and exhibit a dramatic overexpression of two protein disulfide isomerases, PDIA4 and PDIA6.
Txnip (show TXNIP Proteins) is located in the endoplasmic reticulum and interacts with endogenous PDIA6. Txnip (show TXNIP Proteins) increases PDI (show PADI1 Proteins) activity.
levels of expression of ERp5 and GRP78 (show HSPA5 Proteins) correlated with the level of expression of membrane-bound MICA (show MICA Proteins) in chronic lymphocytic leukemia patients.
Data show that the lymph node (LN) stroma displayed in situ high levels of transcription and expression of the disulfide-isomerase ERp5 and of the disintegrin-metalloproteinase (show ADAM17 Proteins) ADAM10 (show ADAM10 Proteins), able to shed the ligands for NKG2D (NKG2D (show KLRK1 Proteins)-L) from the cell membrane.
P5 forms a non-covalent complex with immunoglobulin heavy chain binding protein (BiP (show HSPA5 Proteins)) and shows specificity towards BiP (show GDF10 Proteins) client proteins.
Protein disulfide isomerases (EC 188.8.131.52), such as PDIA6, are endoplasmic reticulum (ER) resident proteins that catalyze formation, reduction, and isomerization of disulfide bonds in proteins and are thought to play a role in folding of disulfide-bonded proteins (Hayano and Kikuchi, 1995
protein disulfide isomerase-related protein
, protein disulfide-isomerase A6
, thioredoxin domain containing 7
, thioredoxin domain-containing protein 7
, ER protein 5
, endoplasmic reticulum protein 5
, protein disulfide isomerase P5
, protein disulfide isomerase-associated 6
, thioredoxin domain containing 7 (protein disulfide isomerase)
, calcium-binding protein 1
, protein disulfide isomerase A6
, protein disulfide isomerase associated 6