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Mouse Anti-GPD1 ( AA 1-349 ) Monoclonal Antibody (CBFYH-2981) (CBMAB-H1312-FY)

This product is mouse antibody that recognizes GPD1. The antibody CBFYH-2981 can be used for immunoassay techniques such as: ELISA, WB.
See all GPD1 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYH-2981
Antibody Isotype
IgG1, κ
Application
ELISA, WB

Basic Information

Immunogen
Full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-349

Target

Full Name
glycerol-3-phosphate dehydrogenase 1 (soluble)
Introduction
This gene encodes a member of the NAD-dependent glycerol-3-phosphate dehydrogenase family. The encoded protein plays a critical role in carbohydrate and lipid metabolism by catalyzing the reversible conversion of dihydroxyacetone phosphate (DHAP) and reduced nicotine adenine dinucleotide (NADH) to glycerol-3-phosphate (G3P) and NAD+. The encoded cytosolic protein and mitochondrial glycerol-3-phosphate dehydrogenase also form a glycerol phosphate shuttle that facilitates the transfer of reducing equivalents from the cytosol to mitochondria. Mutations in this gene are a cause of transient infantile hypertriglyceridemia. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
Entrez Gene ID
2819
UniProt ID
P21695
Alternative Names
Glycerol-3-Phosphate Dehydrogenase 1; Glycerol-3-Phosphate Dehydrogenase 1 (Soluble); EC 1.1.1.8; GPDH-C; GPD-C; Glycerol-3-Phosphate Dehydrogenase [NAD(+)], Cytoplasmic
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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