Human Recombinant GPD1 protein, His Tag (V2LY-0526-LY4337)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant GPD1 protein, His Tag consist of Amino Acid: 1-349 and predicts a molecular mass of 39.4 kDa.
Molecule Mass
39.4 kDa
Sequence
Amino Acid: 1-349
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>95% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
glycerol-3-phosphate dehydrogenase 1 (soluble)
Function
Has glycerol-3-phosphate dehydrogenase activity.
Biological Process
Cellular response to cAMP Source: Ensembl
Cellular response to tumor necrosis factor Source: Ensembl
Gluconeogenesis Source: Ensembl
Glycerol-3-phosphate catabolic process Source: InterPro
Glycerol-3-phosphate metabolic process Source: GO_Central
Glycerolipid metabolic process Source: Ensembl
Glycerophosphate shuttle Source: Ensembl
NADH oxidation Source: GO_Central
Positive regulation of glycolytic process Source: Ensembl
Cellular Location
Cytoplasm
Involvement in disease
Hypertriglyceridemia, transient infantile (HTGTI):
An autosomal recessive disorder characterized by onset of moderate to severe transient hypertriglyceridemia in infancy that normalizes with age. The hypertriglyceridemia is associated with hepatomegaly, moderately elevated transaminases, persistent fatty liver, and the development of hepatic fibrosis.

Pallapati, A. R., Prasad, S., & Roy, I. (2022). Glycerol 3-phosphate dehydrogenase regulates heat shock response in Saccharomyces cerevisiae. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1869(5), 119238.

Luo, Z., Chen, Z., Zhu, Z., Hao, Y., Feng, J., Luo, Q., ... & Ding, G. (2022). Angiotensin II induces podocyte metabolic reprogramming from glycolysis to glycerol-3-phosphate biosynthesis. Cellular Signalling, 99, 110443.

Karaosmanoglu Yoneten, K., Kasap, M., Arga, K. Y., Akpinar, G., & Utkan, N. Z. (2022). Decreased serum levels of glycerol-3-phosphate dehydrogenase 1 and monoacylglycerol lipase act as diagnostic biomarkers for breast cancer. Cancer Biomarkers, 34(1), 67-76.

Pallapati, A. R., Sirigiri, S. D., Jain, S., Ratnala, V., & Roy, I. (2021). Lysine245 plays a crucial role in stability and function of glycerol 3‐phosphate dehydrogenase (Gpd1) in Saccharomyces cerevisiae. Journal of Cellular Biochemistry, 122(11), 1726-1736.

Matarazzo, L., Ragnoni, V., Malaventura, C., Leon, A., Colavito, D., Vigna, G. B., ... & Maggiore, G. (2020). Successful fenofibrate therapy for severe and persistent hypertriglyceridemia in a boy with cirrhosis and glycerol‐3‐phosphate dehydrogenase 1 deficiency. JIMD reports, 54(1), 25-31.

Yoneten, K. K., Kasap, M., Akpinar, G., Gunes, A., Gurel, B., & Utkan, N. Z. (2019). Comparative proteome analysis of breast cancer tissues highlights the importance of glycerol-3-phosphate dehydrogenase 1 and monoacylglycerol lipase in breast cancer metabolism. Cancer Genomics & Proteomics, 16(5), 377-397.

Lee, J., & Levin, D. E. (2019). Methylated metabolite of arsenite blocks glycerol production in yeast by inhibition of glycerol-3-phosphate dehydrogenase. Molecular Biology of the Cell, 30(17), 2134-2140.

Chhikara, S., Abdullah, H. M., Akbari, P., Schnell, D., & Dhankher, O. P. (2018). Engineering Camelina sativa (L.) Crantz for enhanced oil and seed yields by combining diacylglycerol acyltransferase1 and glycerol‐3‐phosphate dehydrogenase expression. Plant biotechnology journal, 16(5), 1034-1045.

Li, J. Q., Xie, X. B., Feng, J. Y., Chen, L., Abuduxikuer, K., Lu, Y., ... & Wang, J. S. (2018). A novel homozygous mutation in the glycerol-3-phosphate dehydrogenase 1 gene in a Chinese patient with transient infantile hypertriglyceridemia: a case report. BMC gastroenterology, 18(1), 1-8.

Mojardín, L., Vega, M., Moreno, F., Schmitz, H. P., Heinisch, J. J., & Rodicio, R. (2018). Lack of the NAD+-dependent glycerol 3-phosphate dehydrogenase impairs the function of transcription factors Sip4 and Cat8 required for ethanol utilization in Kluyveromyces lactis. Fungal Genetics and Biology, 111, 16-29.

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For research use only. Not intended for any clinical use.

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