PDIA6 Recombinant Monoclonal Antibody

1. Results indicate that protein disulfide isomerase family 6 (PDIA6) overexpression promoted the proliferation of HeLa cells by suppressing the phosphorylation of beta-catenin, thereby inhibiting the degradation of beta-catenin through the ubiquitin-proteasome pathway. PMID: 27462866
2. the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition. PMID: 28949004
3. 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/beta-catenin signaling pathway. PMID: 27760590
4. Results indicate that re-expression of miR-127-3p and miR-376a-3p induces a strong tumor suppressor effect in GCTSC, which is partially mediated via COA1 and PDIA6. PMID: 28866093
5. ACE and PDIA6 were identified as potential HSPA2-interacting proteins; this assemblage resides in membrane raft microdomains located in the peri-acrosomal region of the sperm head. PMID: 26676989
6. Restoration of miR-127-3p and miR-376a-3p counteracts the neoplastic phenotype of giant cell tumor of bone derived stromal cells by targeting COA1, GLE1 and PDIA6. PMID: 26655997
7. PDIA3 and PDIA6 gene expression is a neoplasm aggressiveness marker in primary ductal breast cancer. PMID: 26125904
8. 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. PMID: 24464223
9. Txnip is located in the endoplasmic reticulum and interacts with endogenous PDIA6. Txnip increases PDI activity. PMID: 24843047
10. levels of expression of ERp5 and GRP78 correlated with the level of expression of membrane-bound MICA in chronic lymphocytic leukemia patients. PMID: 22215138
11. 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 ADAM10, able to shed the ligands for NKG2D (NKG2D-L) from the cell membrane. PMID: 22167753
12. P5 forms a non-covalent complex with immunoglobulin heavy chain binding protein (BiP) and shows specificity towards BiP client proteins. PMID: 19887585
13. observed to have peptide-binding ability, and chaperone activity was confirmed with rhodanese and citrate synthase as substrates, but not with D-glyceraldehyde-3-phosphate dehydrogenase, showing substrate specificity with respect to chaperone activity PMID: 12204115
14. ERP5 regulates the binding of fibrinogen, cell-surface exposure of P-selectin, and coassociation of beta 3 integrin in stimulated platelets. PMID: 15466936
15. Pharmacological inhibition of thioreductase activity and ERp5 gene silencing revealed that cell-surface ERp5 function is required for MICA shedding PMID: 17495932

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HGNC: 30168

OMIM: 611099

KEGG: hsa:10130

STRING: 9606.ENSP00000272227

UniGene: Hs.212102