GLUD1 + GLUD2 antibody
GTX105765
ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
Product group Antibodies
ReactivityDrosophila, Human, Mouse, Rat
TargetGLUD1
Overview
- SupplierGeneTex
- Product NameGLUD1 + GLUD2 antibody
- Delivery Days Customer9
- Application Supplier NoteWB: 1:500-1:3000. ICC/IF: 1:100-1:1000. IHC-P: 1:100-1:1000. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.
- ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry, ImmunoHistoChemistry Paraffin
- CertificationResearch Use Only
- ClonalityPolyclonal
- Concentration0.07 mg/ml
- ConjugateUnconjugated
- Gene ID2746
- Target nameGLUD1
- Target descriptionglutamate dehydrogenase 1
- Target synonymsGDH, GDH1, GLUD, hGDH1, glutamate dehydrogenase 1, mitochondrial, epididymis secretory sperm binding protein, epididymis tissue sperm binding protein Li 18mP, glutamate dehydrogenase (NAD(P)+)
- HostRabbit
- IsotypeIgG
- Protein IDP00367
- Protein NameGlutamate dehydrogenase 1, mitochondrial
- Scientific DescriptionL-glutamate dehydrogenase (EC 1.4.1.3) has a central role in nitrogen metabolism in plants and animals. Glutamate dehydrogenase is found in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate (Smith et al., 2001 [PubMed 11254391]). Glutamate, the main substrate of GLUD, is present in brain in concentrations higher than in other organs. In nervous tissue, GLUD appears to function in both the synthesis and the catabolism of glutamate and perhaps in ammonia detoxification (Mavrothalassitis et al., 1988 [PubMed 3368458]).[supplied by OMIM]
- ReactivityDrosophila, Human, Mouse, Rat
- Storage Instruction-20°C or -80°C,2°C to 8°C
- UNSPSC12352203
References
- Geiszler PC, Ugun-Klusek A, Lawler K, et al. Dynamic metabolic patterns tracking neurodegeneration and gliosis following 26S proteasome dysfunction in mouse forebrain neurons. Sci Rep. 2018,8(1):4833. doi: 10.1038/s41598-018-23155-2Read this paper
- Gonzalez SN, Valsecchi WM, Maugeri D, et al. Structure, kinetic characterization and subcellular localization of the two ribulose 5-phosphate epimerase isoenzymes from Trypanosoma cruzi. PLoS One. 2017,12(2):e0172405. doi: 10.1371/journal.pone.0172405Read this paper
- Cho CK, Smith CR, Diamandis EP. Amniotic fluid proteome analysis from Down syndrome pregnancies for biomarker discovery. J Proteome Res. 2010,9(7):3574-82. doi: 10.1021/pr100088kRead this paper


