anti-Kruppel-Like Factor 3 (Basic) (KLF3) Antikörper

Cow (Bovine) Kruppel-Like Factor 3 (Basic) (KLF3) Interaktionspartner

1. 3 SNPs in the bovine KLF3 gene promoter region, which mainly regulate the transcription initiation of the gene and combine the transcription factors to regulate gene transcription activity.

Human Kruppel-Like Factor 3 (Basic) (KLF3) Interaktionspartner

1. These data demonstrate that miR-326/Sp1/KLF3 regulatory axis is involved in the development of lung cancer. miR-326 could bind to 3'UTR of Sp1 but not KLF3 and decreased the accumulation of Sp1, which further indirectly reduced KLF3 expression and inactivated JAK2/STAT3 and PI3K/AKT signaling pathways in vitro and in vivo.

2. Low KLF3 expression is associated with colorectal cancer.

3. Among the mechanosensitive genes, the two transcription factors, HoxA5 and Klf3, contain cAMP-response-elements methylation of which could serve as a mechanosensitive master switch in gene expression in atherosclerosis. (Review)

4. Klf-3 expression is downregulated in human metastatic sarcomas, and Klf-3 levels negatively correlate with miR-182 expression.

5. A feedback loop consisting of microRNA 23a/27a and the beta-like globin suppressors KLF3 and SP1 regulates globin gene expression.

6. B cell differentiation is significantly impaired in the bone marrow, spleen, and peritoneal cavity of Klf3 null mice; the defects are cell autonomous.

7. Low KLF3 is associated with acute myeloid leukemia.

8. KLF3 is an important regulator of several biological processes, including adipogenesis, erythropoiesis, and B cell development. (Review)

9. The recruitment of CtBP and sumoylation are required for full repression by BKLF.

Mouse (Murine) Kruppel-Like Factor 3 (Basic) (KLF3) Interaktionspartner

1. KLF1 and KLF3 bind common as well as unique sites within the erythroid cell genome.

2. mechanistic insights into the regulation of Lgals3, demonstrating that C-terminal binding protein (CtBP) is required to drive optimal KLF3-mediated silencing.

3. Cineromycin B inhibited adipocyte differentiation in 3T3-L1 cells mainly via upregulation of KLF2 and KLF3 mRNA expression at an early stage of the differentiation.

4. Phosphorylation of KLF3 and CtBP2 by HIPK2 strengthens the interaction between these two factors and increases transcriptional repression by KLF3.

5. KLF3 acts as transcriptional repressor for the leukocyte-specific integrin beta7 (Itgb7, Ly69) by binding to the beta7 promoter, as revealed by chromatin immunoprecipitation.

6. We conclude that KLF3 plays diverse and important roles in cardiovascular development and function in mice.

7. KLF3 binds the Fam132a promoter in vitro and in vivo and that this leads to repression of promoter activity. Fam132a is significantly upregulated in the absence of KLF3.

8. KLF3 and KLF8 have overlapping roles in vivo and participate in the silencing of embryonic globin expression during development.

9. IL-17 suppresses expression of PPARgamma, C/EBPalpha, KLF15, a pro-adipogenic transcription factor, and enhances expression of KLF2 and KLF3, which are anti-adipogenic.

10. KLF3 is a feedback repressor that counters the activity of EKLF at selected target genes to achieve normal erythropoiesis

11. we concluded that KLF3 is a transcriptional repressor for wee1 gene.

12. KLF3 is a driving force toward marginal zone B-cell maturation.

13. KLF3 is an important regulator of several biological processes, including adipogenesis, erythropoiesis, and B cell development. (Review)

14. role for KLF3 in muscle gene regulation and an alternate mechanism for transcriptional regulation by SRF via its recruitment to KLF binding sites

15. Proviral integration of an Abelson-murine leukemia virus deregulates BKLF-expression in the hypermutating pre-B cell line 18-81.

16. in erythroid tissues basic Kruppel-like factor (Bklf/Klf3) expression is highly dependent on another family member, erythroid Kruppel-like factor (Eklf/Klf1)

17. basic Kruppel-like factor gene (Klf3) has a role with CtBP in adipogenesis

18. Klf8 is repressed by Klf3 and activated by Klf1 in vivo.