Transfected Stable Cell Lines
Reliable | High-Performance | Wide Rage
Precision reporter, kinase, immune receptor, biosimilar, Cas9, and knockout stable cell lines for diverse applications.
| Cat.No. | Product Name | Price |
|---|---|---|
| CSC-DC003032 | Panoply™ Human CFH Knockdown Stable Cell Line | Inquiry |
| CSC-DC005730 | Panoply™ Human FH Knockdown Stable Cell Line | Inquiry |
| CSC-DC008617 | Panoply™ Human LDLR Knockdown Stable Cell Line | Inquiry |
| CSC-SC003032 | Panoply™ Human CFH Over-expressing Stable Cell Line | Inquiry |
| CSC-SC005730 | Panoply™ Human FH Over-expressing Stable Cell Line | Inquiry |
| CSC-SC008617 | Panoply™ Human LDLR Over-expressing Stable Cell Line | Inquiry |
| CLOE-1235 | Human CFH HEK293 Cell Lysate | Inquiry |
| CLOE-1589 | Human LDLR HEK293 Cell Lysate | Inquiry |
| CLOE-2241 | Mouse Cfh HEK293 Cell Lysate | Inquiry |
| CLOE-2242 | Mouse Cfh(Fc) HEK293 Cell Lysate | Inquiry |
| CLKO-0732 | FH KO Cell Lysate-HEK293T | Inquiry |
| CSC-RT2645 | Human LDLR Knockout Cell Line-HEK293T | Inquiry |
| CSC-RT2986 | Human LDLR KO Cell Line-HeLa | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| AD00353Z | LDLR adenovirus | Inquiry |
| AD03616Z | Human Cfh adenoviral particles | Inquiry |
| AD09091Z | Human LDLR adenoviral particles | Inquiry |
| LV08861L | human CFH (NM_000186) lentivirus particles | Inquiry |
| LV08862L | human CFH (NM_001014975) lentivirus particles | Inquiry |
| LV12872L | human FH (NM_000143) lentivirus particles | Inquiry |
| LV16859L | human LDLR (NM_001195803) lentivirus particles | Inquiry |
| LV16860L | human LDLR (NM_001195798) lentivirus particles | Inquiry |
| LV16861L | human LDLR (NM_001195799) lentivirus particles | Inquiry |
| LV16862L | human LDLR (NM_000527) lentivirus particles | Inquiry |
| LV16863L | human LDLR (NM_001195802) lentivirus particles | Inquiry |
| LV16864L | human LDLR (NM_001195800) lentivirus particles | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SHG169093 | shRNA set against Rat Cfh(NM_130409.2) | Inquiry |
| SHH145533 | shRNA set against Rat Ldlr(NM_175762.2) | Inquiry |
| SHH329344 | shRNA set against Rat LDLR (NM_175762.2) | Inquiry |
| SHG169297 | shRNA set against Mouse Cfh(NM_009888.3) | Inquiry |
| SHH262417 | shRNA set against Human Cfh (NM_000186.3) | Inquiry |
| SHH262421 | shRNA set against Mouse Cfh (NM_009888.3) | Inquiry |
| SHH294801 | shRNA set against Mouse FH (NM_175276.3) | Inquiry |
| SHH329335 | shRNA set against Human LDLR (NM_000527.4) | Inquiry |
| SHH329339 | shRNA set against Mouse LDLR (NM_010700.3) | Inquiry |
| SHW000466 | shRNA set against Chicken FH (NM_001006382) | Inquiry |
| SHW004965 | shRNA set against Chicken LDLR (NM_204452) | Inquiry |
| SHW013733 | shRNA set against Danio rerio CFH (NM_001199190) | Inquiry |
| SHW017084 | shRNA set against Danio rerio FH (NM_200963) | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SKO0479 | FH Validated sgRNA vector | Inquiry |
| CDCL151278 | Mouse Ldlr ORF clone (NM_001252659.1) | Inquiry |
| CDFL002638 | Mouse Cfh cDNA Clone(NM_009888.3) | Inquiry |
| CDFR011075 | Rat Fh cDNA Clone(NM_017005.2) | Inquiry |
| CDFR013884 | Rat Cfh cDNA Clone(NM_130409.2) | Inquiry |
| CDFR014870 | Rat Ldlr cDNA Clone(NM_175762.2) | Inquiry |
| MiUTR3H-08845 | LDLR miRNA 3'UTR clone | Inquiry |
| MiUTR1M-02968 | CFH miRNA 3'UTR clone | Inquiry |
| CDCL126663 | Human LDLR ORF clone (NM_001195799.1) | Inquiry |
| MiUTR1R-01907 | FH miRNA 3'UTR clone | Inquiry |
| MiUTR1R-02978 | LDLR miRNA 3'UTR clone | Inquiry |
| CDCB178559 | Danio rerio FH ORF Clone (NM_200963) | Inquiry |
| MiUTR3H-00770 | CFH miRNA 3'UTR clone | Inquiry |
| MiUTR3H-00771 | CFH miRNA 3'UTR clone | Inquiry |
| CDCB161941 | Chicken FH ORF Clone (NM_001006382) | Inquiry |
| MiUTR3H-00833 | FH miRNA 3'UTR clone | Inquiry |
| MiUTR1R-00949 | CFH miRNA 3'UTR clone | Inquiry |
| CDCS405486 | Human CFH ORF Clone (BC037285) | Inquiry |
| CDCS405453 | Human FH ORF Clone (BC003108) | Inquiry |
| CDCR381787 | Rat Ldlr ORF Clone(NM_175762.2) | Inquiry |
| CDCR380918 | Rat Cfh ORF Clone(NM_130409.2) | Inquiry |
| CDCR046344 | Human CFH ORF clone (NM_001014975.2) | Inquiry |
| CDCR046346 | Mouse Cfh ORF clone (NM_009888.3) | Inquiry |
| CDCB157200 | Mouse LDLR ORF clone (NM_010700.2) | Inquiry |
| CDCB166440 | Chicken LDLR ORF Clone (NM_204452) | Inquiry |
| CDCB175208 | Danio rerio CFH ORF Clone (NM_001199190) | Inquiry |
| CDCB180785 | Rabbit LDLR ORF clone (NM_001278865.1) | Inquiry |
| CDCB181791 | Rabbit C3H5orf46 ORF clone (XM_008255203.1) | Inquiry |
| CDCB183347 | Rabbit FH ORF clone (XM_002717334.2) | Inquiry |
| CDCR378118 | Rat Fh ORF Clone(NM_017005.2) | Inquiry |
| CDCB193526 | Rabbit CFH ORF clone (XM_008268719.1) | Inquiry |
| CDCL126667 | Mouse LDLR ORF clone (NM_001195798.1) | Inquiry |
| CDCL126669 | Mouse LDLR ORF clone (NM_001195800.1) | Inquiry |
| CDCL126671 | Human LDLR ORF clone (NM_001195802.1) | Inquiry |
| CDCL151276 | Mouse Ldlr ORF clone (NM_001252658.1) | Inquiry |
| CDCL183534 | Human CFH ORF clone(NM_000186.3) | Inquiry |
| CDCL184279 | Human FH ORF clone(NM_000143.3) | Inquiry |
| CDCL126665 | Human LDLR ORF clone (NM_001195803.1) | Inquiry |
| CDCB156200 | Rat CFH ORF clone (BC089845.1) | Inquiry |
Fumarate hydratase (FH) catalyzes the reversible hydration reaction of fumarate to L-malic acid, which is widely present in animals, plants and microorganisms. FH is expressed in both mitochondria and cytoplasm. While participating in the tricarboxylic acid cycle (TCA) in the mitochondria, it also participates in the metabolism of fumaric acid in the cytoplasm to regulate fumaric acid levels. Loss of FH gene will cause many human diseases. For example, fumarate hydratase deficiency is an autosomal recessive genetic disease, manifested as metabolic disorders, severe encephalopathy, seizures and poor neurological prognosis. A large number of studies have shown that gene mutations of enzymes involved in the tricarboxylic acid cycle may cause the occurrence and development of tumors.
Fumarate hydratase is an enzyme in the tricarboxylic acid cycle, which mainly catalyzes the hydration of fumarate to form L-malic acid. The catalytic reaction of the enzyme is reversible, but has strict stereoselectivity. The hydroxyl group that cleaves is strictly added to one side of the double bond of the fumaric acid molecule, and hydrogen is added to the other side. Therefore, in the reaction, it only catalyzes the hydration of the trans-double-shoulder (fumaric acid), but not maleic acid. The reverse reaction only catalyzes the formation of the L-isomer of silicic acid. Fumarate hydratase belongs to a family of homologous enzymes containing similar amino acid sequences. It is a key enzyme involved in energy metabolism.
Multiple skin and uterine leiomyoma syndrome (MCUL) is an autosomal dominant hereditary tumor susceptibility disease, which mainly occurs in the skin and uterine smooth muscle. When associated with renal cell carcinoma, this syndrome is called hereditary leiomyoma and renal cell carcinoma (HLRCC). Mutations in FH cause hereditary skin leiomyomas and have specific correlations. Studies on families with HLRCC found that approximately one-third of patients have kidney cancer. Studies have shown that when the fumarate hydratase gene is lacking, fumarate accumulates, which activates an abnormal physiological pathway in uterine muscle cells, thereby causing uterine fibroids.
Fig1 False hypoxia-driven mechanism of HLRCC
The pathogenic mechanism of HLRCC is related to pseudo-hypoxic drive. Pseudo-hypoxic drive refers to the activation of hypoxia signaling pathways under conditions of re-hypoxia. Studies have confirmed that the expression levels of HIF-1α and HIF-2α in HLRCC tumor cells are significantly increased. HIF is a key regulator for regulating oxygen balance. Strict regulation of HIF under hypoxic conditions can ensure the survival and growth of cells. HIF regulates vascular endothelial growth factor (VEGF), platelet derived growth factor (PDGF), vascular endothelial growth factor receptor (EGFR), glucose transporter 1 Glucose Transporter Protein (GTP1), crude erythropoietin, transforming growth factor-α. Fumarate and succinate are competitive inhibitors of multiple α-ketoglutarate-dependent dioxygenases, such as histone demethylase, prolyl hydroxylase, and collagen prolyl 4- Hydroxylase and 5-methylcytosine hydroxylase family. The Von Hippel-Lindau (VHL) complex can specifically bind to HIF-1α and HIF-2α and degrade them. However, the VHL complex can only recognize HIF where the proline residue is hydroxylated. Hydroxylation of the proline residues of HIF requires the participation of prolyl hydroxylase, oxygen molecules and α-ketoglutarate. Under hypoxic conditions, HIF makes it non-hydroxylated, so it can avoid binding to VHL complexes. The accumulation of HIF leads to an increase in downstream glycolysis, a decrease in the mitochondrial respiratory chain and a hierarchical mitochondrial autophagy to avoid normal energy metabolism pathways, which in turn causes the occurrence of tumors.
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