GPD1A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Zebrafish | GPD1A-2467Z | Recombinant Zebrafish GPD1A | Mammalian Cell | His |
- Involved Pathway
- Protein Function
- Interacting Protein
GPD1A involved in several pathways and played different roles in them. We selected most pathways GPD1A participated on our site, such as Glycerophospholipid metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with GPD1A were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Glycerophospholipid metabolism | GNPAT;PCYT1A;PLA2G4F;PCYT1BB;PLD3;PCYT1AB;PLA2G2D;DGKA;LPGAT1 |
GPD1A has several biochemical functions, for example, NAD binding, glycerol-3-phosphate dehydrogenase [NAD+] activity, oxidoreductase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by GPD1A itself. We selected most functions GPD1A had, and list some proteins which have the same functions with GPD1A. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
NAD binding | NDUFS2;DLD;IDH3B;ME1;GPD1L;PHGDH;HIBADHA;HPGD;GPD1C |
glycerol-3-phosphate dehydrogenase [NAD+] activity | TESCA;GPD1B;GPD1A;GPD1C;GPD1;GPD1L |
oxidoreductase activity | VAT1;CYP4A10;TESCA;CYP46A1.4;CYP2N13;AKR1C21;AKR1E1;TDH;SDR16C5A |
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | TESCA;HSD3B6;FAM213B;MDH1B;GPD1;CTBP1;MDH1AA;CTBP2L;HSD3B5 |
protein homodimerization activity | LGALS1;CSF1R;TESC;MCL1B;ASNSD1;BOK;HPRT1;TPD52;Anks6 |
GPD1A has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GPD1A here. Most of them are supplied by our site. Hope this information will be useful for your research of GPD1A.
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