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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 Proteins (13) and TSC22D3 Kits (3) and many more products for this protein.
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Human Polyclonal TSC22D3 Primary Antibody for EIA, WB - ABIN955352
Latré de Laté, Pépin, Assaf-Vandecasteele, Espinasse, Nicolas, Asselin-Labat, Bertoglio, Pallardy, Biola-Vidamment: Glucocorticoid-induced leucine zipper (GILZ) promotes the nuclear exclusion of FOXO3 in a Crm1-dependent manner. in The Journal of biological chemistry 2010
Show all 4 references for ABIN955352
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
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.
Data show a diminished expression of the anti-inflammatory mediator GILZ in the inflamed vasculature and indicate that GILZ downregulation requires the mRNA binding protein ZFP36 (show ZFP36 Antibodies).
Inhibition of epithelial injury repair by dexamethasone is mediated in part by activation of GILZ.
study suggests that GILZ variants are not common causes of SCO (show SNAI1 Antibodies) and NOA (show DLAT Antibodies) in Australian or American men
Exogenous GILZ exerts inhibitory effects on endothelial cell adhesive function via a novel pathway involving modulation of NF-kappaB (show NFKB1 Antibodies) p65 (show GORASP1 Antibodies) DNA binding and MAPK (show MAPK1 Antibodies) activity.
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
We found potential links between the alterations in expression of Tsc22d3, Nfkbia (show NFKBIA Antibodies) and Pdyn (show PDYN Antibodies), and different aspects of susceptibility to stress.
GILZ plays important roles in bone-immune cell communication and BMSC immune suppressive functions.
GILZ is a key factor involved in the immunosuppressive potential of MSCs. MSCs derived from GILZ(-/-) mice did not suppress the proliferation of CD4 (show CD4 Antibodies)+ T cells and were less efficient than MSCs derived from WT mice in altering Th17 cell polarization.
GILZ is expressed during the resolving phase of inflammation in macrophages with proresolving phenotypes
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