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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. Zusätzlich bieten wir Ihnen TSC22D3 Kits (19) und TSC22D3 Proteine (14) und viele weitere Produktgruppen zu diesem Protein an.
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Human Monoclonal TSC22D3 Primary Antibody für 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 (zeige LEP Antikörper) and leptin receptor (zeige LEPR Antikörper) 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 (zeige TNF Antikörper) 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 (zeige BCL2L1 Antikörper) level. GILZ protein affects the unfolded protein response signaling shifting the balance towards pro-survival signals as judged by down-regulation of CHOP (zeige DDIT3 Antikörper), ATF4 (zeige ATF4 Antikörper), XBP1s mRNA and increase in GRP78 (zeige HSPA5 Antikörper) protein level.
results reveal GILZ to be a new actor in apoptosis regulation in neutrophil-like cells involving JNK (zeige MAPK8 Antikörper) and Mcl-1 (zeige MCL1 Antikörper).
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 (zeige TP53 Antikörper) proteins by decreasing p53 (zeige TP53 Antikörper) ubiquitination and increasing MDM2 (zeige MDM2 Antikörper) 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 (zeige SLC12A3 Antikörper) and enhancing distal sodium delivery to the epithelial sodium channel.
HuR (zeige ELAVL1 Antikörper) 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 (zeige ANXA1 Antikörper) by GCs (zeige UGCG Antikörper). As Anxa1 (zeige ANXA1 Antikörper) 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 (zeige IL17A Antikörper))-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