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The protein encoded by TSC22D3 shares significant sequence identity with the murine TSC-22 and Drosophila shs, both of which are leucine zipper proteins, that function as transcriptional regulators. Additionally we are shipping TSC22D3 Kits (19) and TSC22D3 Proteins (14) and many more products for this protein.
Showing 10 out of 103 products:
Human Monoclonal TSC22D3 Primary Antibody for ELISA, WB - ABIN515084
Srinivasan, Janardhanam: Novel p65 binding glucocorticoid-induced leucine zipper peptide suppresses experimental autoimmune encephalomyelitis. in The Journal of biological chemistry 2011
Zebrafish tsc22d3 is a ventralizing gene and plays a role in early embryogenesis
We propose a novel role of GILZ in contributing to corticoid-induced leptin (show LEP Antibodies) and leptin receptor (show LEPR Antibodies) expression in osteoarthritis synovial fibroblasts
TSC22D3 gene expression is significantly associated with long-term changes in Blood Pressure, providing a link between gene expression and Blood Pressure.
Overall, these results suggest that GILZ antagonizes the pro-inflammatory effects of TNFa (show TNF Antibodies) in human adipocytes, and its downregulation in obesity may contribute to adipose inflammation and dysregulated adipokine production, and thereby systemic metabolism.
Under endoplasmic reticulum stress conditions, overexpression of GILZ significantly reduced activation of mitochondrial pathway of apoptosis by maintaining Bcl-xl (show BCL2L1 Antibodies) level. GILZ protein affects the unfolded protein response signaling shifting the balance towards pro-survival signals as judged by down-regulation of CHOP (show DDIT3 Antibodies), ATF4 (show ATF4 Antibodies), XBP1s mRNA and increase in GRP78 (show HSPA5 Antibodies) protein level.
results reveal GILZ to be a new actor in apoptosis regulation in neutrophil-like cells involving JNK (show MAPK8 Antibodies) and Mcl-1 (show MCL1 Antibodies).
GILZ is a non-redundant regulator of B cell activity, with important potential clinical implications in systemic lupus erythematosus.
our data suggest that GILZ is a key regulator of macrophage functions.
L-GILZ stabilizes p53 (show TP53 Antibodies) proteins by decreasing p53 (show TP53 Antibodies) ubiquitination and increasing MDM2 (show MDM2 Antibodies) ubiquitination.
The N-terminal part of L-GILZ protein is responsible for Ras/L-GILZ protein-to-protein interaction, important for the control of proliferation rate of spermatogonia.
PUVA directly stimulates GILZ expression.
GILZ promotes potassium secretion by inhibiting sodium-chloride cotransporter (show SLC12A3 Antibodies) and enhancing distal sodium delivery to the epithelial sodium channel.
HuR (show ELAVL1 Antibodies) overexpression led to increased GILZ protein levels but had no effect on GILZ mRNA expression.
The present findings shed light on the role of GILZ in the mechanism of induction of Anxa1 (show ANXA1 Antibodies) by GCs (show UGCG Antibodies). As Anxa1 (show ANXA1 Antibodies) is an important protein for the resolution of inflammatory response, GILZ may represent a new pharmacologic target for treatment of inflammatory diseases.
Role of glucocorticoid-induced leucine zipper (GILZ) in inflammatory bone loss
marked reduction in cardiac GILZ in association with increased Th-17 cells accompanied with marked disruption of mitochondrial membrane potential and increased apoptotic/necrotic cell death in hearts subjected to myocardial infarction
results identify GILZ as an endogenous inhibitor of macropinocytosis in DCs, the action of which contributes to the fine-tuning of Ag cross-presentation.
Obesity is associated with a downregulation of the Gr-Gilz axis in kupffer cells, which promotes liver inflammation.
Data show that glucocorticoid-induced leucine zipper (GILZ) maintains a threshold for activation of Th17 responses and interleukin 17 (IL-17 (show IL17A Antibodies))-dependent pathology.
Lack of glucocorticoid-induced leucine zipper deregulates B-cell survival and results in B-cell lymphocytosis
The protein encoded by this gene shares significant sequence identity with the murine TSC-22 and Drosophila shs, both of which are leucine zipper proteins, that function as transcriptional regulators. The expression of this gene is stimulated by glucocorticoids and interleukin 10, and it appears to play a key role in the anti-inflammatory and immunosuppressive effects of this steroid and chemokine. Transcript variants encoding different isoforms have been identified for this gene.
TSC22 domain family, member 3
, glucocorticoid-induced leucine zipper
, TSC22 domain family protein 3
, glucocorticoid-induced leucine zipper protein
, DSIP-immunoreactive leucine zipper protein
, DSIP-immunoreactive peptide
, TSC-22 related protein
, TSC-22-like protein
, TSC-22-related protein
, delta sleep inducing peptide, immunoreactor
, delta sleep-inducing peptide immunoreactor
, TSC22 domain family 3
, TSC22-related inducible leucine zipper 3
, TSC22-related-inducible leucine zipper 3
, long glucocorticoid-induced leucine zipper protein
, DIP protein
, Glucocorticoid-induced leucine zipper protein
, delta-sleep-inducing peptide