

| Catalog No. | HY347014 | ||||||||
|---|---|---|---|---|---|---|---|---|---|
| Description |
Anti-DLD Polyclonal Antibody (HY347014) is a rabbit polyclonal antibody detecting DLD in ELISA, IHC, WB. Suitable for Human, Mouse, Dog, Rat, and Bovine.
Highlights
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| Species reactivity | Human, Mouse, Rat | ||||||||
| Applications | ELISA, IHC, WB | ||||||||
| Host species | Rabbit | ||||||||
| Isotype | IgG | ||||||||
| Clonality | Polyclonal | ||||||||
| Immunogen | E. coli - derived recombinant Human DLD (Lys283-His487). | ||||||||
| Target | Glycine cleavage system L protein, Dihydrolipoamide dehydrogenase, GCSL, DLD, PHE3, Dihydrolipoyl dehydrogenase, mitochondrial, LAD | ||||||||
| Purification | Purified by antigen affinity column. | ||||||||
| Accession | P09622 | ||||||||
| Form | Liquid | ||||||||
| Storage buffer | 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA. |
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| Product Usage Information |
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| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. | ||||||||
| Background | Dihydrolipoyl dehydrogenase, mitochondrial (DLD) is a ~54 kDa protein. Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A. In monomeric form may have additional moonlighting function as serine protease. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction. 1. Odièvre, MH. et al. (2005) Human mutation 25, 323-4. PMID: 15712224 2. Brautigam, CA. et al. (2006) Structure (London, England : 1993) 14, 611-21. PMID: 16442803 3. Cameron, JM. et al. (2006) American journal of medical genetics. Part A 140, 1542-52. PMID: 16770810 4. Babady, NE. et al. (2007) Proceedings of the National Academy of Sciences of the United States of America 104, 6158-63. PMID: 17404228 5. Patel, MS. et al. (2009) Journal of molecular catalysis. B, Enzymatic 61, 2-6. PMID: 20160912 6. Park, YH. et al. (2010) Biochemical and biophysical research communications 395, 416-9. PMID: 20385101 7. Wang, Y. et al. (2017) Nature 552, 273-277. PMID: 29211711 | ||||||||
| Note | For research use only. |
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