Transfected Stable Cell Lines
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Precision reporter, kinase, immune receptor, biosimilar, Cas9, and knockout stable cell lines for diverse applications.
| Cat.No. | Product Name | Price |
|---|---|---|
| CSC-DC001396 | Panoply™ Human BDH1 Knockdown Stable Cell Line | Inquiry |
| CSC-SC001396 | Panoply™ Human BDH1 Over-expressing Stable Cell Line | Inquiry |
| CSC-SC001396-1 | Human BDH1 Stable Cell Line - HEK293 | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| AD01782Z | Human BDH1 adenoviral particles | Inquiry |
| LV06196L | human BDH1 (NM_203314) lentivirus particles | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| SHG098659 | shRNA set against Human BDH1(NM_004051.4) | Inquiry |
| SHH246194 | shRNA set against Mouse BDH1 (NM_175177.4) | Inquiry |
| SHH246198 | shRNA set against Rat BDH1 (NM_053995.3) | Inquiry |
| SHW000627 | shRNA set against Chicken BDH1 (NM_001006547) | Inquiry |
| SHW011490 | shRNA set against Danio rerio BDH1 (NM_001089509) | Inquiry |
| Cat.No. | Product Name | Price |
|---|---|---|
| CDCB180919 | Rabbit BDH1 ORF clone (XM_002716523.2) | Inquiry |
| CDFG013426 | Human BDH1 cDNA Clone(NM_203314.2) | Inquiry |
| CDFG013427 | Human BDH1 cDNA Clone(NM_203315.2) | Inquiry |
| CDFR013697 | Rat Bdh1 cDNA Clone(NM_053995.3) | Inquiry |
| MiUTR1H-00862 | BDH1 miRNA 3'UTR clone | Inquiry |
| MiUTR1R-00544 | BDH1 miRNA 3'UTR clone | Inquiry |
| CDCB158764 | Human BDH1 ORF clone (BC011964) | Inquiry |
| CDCB162102 | Chicken BDH1 ORF Clone (NM_001006547) | Inquiry |
| CDCB172965 | Danio rerio BDH1 ORF Clone (NM_001089509) | Inquiry |
| CDCR034296 | Mouse Bdh1 ORF clone (NM_001122683.1) | Inquiry |
| CDCR272652 | Mouse Bdh1 ORF Clone(NM_175177.4) | Inquiry |
| CDCR327234 | Human BDH1 ORF Clone(NM_203314.2) | Inquiry |
| CDCR327236 | Human BDH1 ORF Clone(NM_203315.2) | Inquiry |
| CDCR380730 | Rat Bdh1 ORF Clone(NM_053995.3) | Inquiry |
| CDCS411581 | Human BDH1 ORF Clone (BC011964) | Inquiry |
D-β-hydroxybutyrate dehydrogenase 1 (BDH1) encodes a member of the short-chain dehydrogenase/reductase gene family. This coding protein forms the homotrimeric enzyme required for positioning in mitochondrial membrane, which has special requirements for the activity of phospholipase. The encoded protein catalyzes the mutual conversion of acetoacetate and (R)-3-hydroxybutyrate, the two major ketone bodies produced during fatty acid catabolism. Alternatively spliced transcript variants encoding the same protein have been described.
BDH1 is Significantly Up-regulated in Overload-Induced Heart Failure
Congestive heart failure is a crucial clinical problem associated with a high mortality rate. Deprivation of cardiac energy metabolism induces cardiac remodeling, ATP production and myocardial energy damage, leading to pathological hypertrophy and heart failure. Many studies have described myocardial metabolism with both glucose and fatty acid utilization in failing hearts. It is well known that cardiac ketone body metabolism is evolutionally conserved and widely used in various organs, which can act as an energy substitute in cases of glucose deprivation. Ketone bodies consist of 3 compounds: acetone, acetoacetate and β-hydroxybutyrate (βOHB), βOHB is reconverted to acetyl-CoA as an energy source. Thus ketone bodies act as a significant energy supplier to avoid energy crisis in the case of impaired glucose or oxygen delivery, for example in advanced heart failure.
After the transverse aortic constriction of the heart, BDH1 expresses an increased enzyme that catalyzes the NAD+/NADH coupled interconversion of acetoacetate and βOHB. In addition, the ketone body oxidation of the aortic transverse heart is elevated. Recent study has shown that BDH1 expression is enhanced in the case of overload-induced heart failure. These data indicate that under the circumstance of BDH1 overexpression, the generation of βOHB is increased, and the utilization of ketone bodies as an alternate fuel source is also increased.
Fig 1. Metabolism of ketone bodies (Zhang J, et al. Journal of Lipid Research. 2018).
Under nutrient limiting conditions, cancer cells reactivate gene expression or metabolic pathways to achieve proliferation. A recent study has determined BDH1 and OXCT1 (3-oxoacid CoA transferase 1) expression levels in transplanted tumors, and found no increase in the expression of BDH1 and OXCT1 in tumors derived from PANC-1 cell xenografts, indicating that ketolysis was not activated in xenograft tumors. In contrast, qRT-PCR result has shown that the expression of of BDH1 and OXCT1 in HeLa cell xenografts are upregulated. Metabolic adaptations, such as reactivation of key ketone catabolism enzymes, may be one of the main reasons for failure of KD (ketogenic diet) therapy on lung cancer cell xenografts. This metabolic adaptation can be observed in nutrient-deficient hepatocellular carcinoma cells that utilize ketone bodies to provide energy and cancer progression. Therefore, studying the potential mechanism of reactivation of gene expression can further enhance the anti-tumor effect of KD therapy.
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