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Mouse Anti-FDFT1 Recombinant Antibody (CBXF-2941) (CBMAB-F3648-CQ)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXF-2941
Antibody Isotype
IgG2a, κ
Application
ELISA

Basic Information

Immunogen
Full length recombinant corresponding to aa1-417 from human FFDFT1 (AAH03573) with GST tag
Specificity
Human
Antibody Isotype
IgG2a, 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
Buffer
PBS, pH 7.2
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
farnesyl-diphosphate farnesyltransferase 1
Introduction
This gene encodes a membrane-associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two-step reaction to form squalene.
Entrez Gene ID
2222
UniProt ID
P37268
Alternative Names
Farnesyl-Diphosphate Farnesyltransferase 1; FPP:FPP Farnesyltransferase; Squalene Synthase; EC 2.5.1.21; SQS; SS;
Research Area
Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene. Proceeds in two distinct steps. In the first half-reaction, two molecules of FPP react to form the stable presqualene diphosphate intermediate (PSQPP), with concomitant release of a proton and a molecule of inorganic diphosphate. In the second half-reaction, PSQPP undergoes heterolysis, isomerization, and reduction with NADPH or NADH to form squalene. It is the first committed enzyme of the sterol biosynthesis pathway.
Biological Process
Cholesterol biosynthetic process Source: GO_Central
Farnesyl diphosphate metabolic process Source: GO_Central
Steroid biosynthetic process Source: ProtInc
Cellular Location
Endoplasmic reticulum membrane
Involvement in disease
An autosomal recessive disorder characterized by profound developmental delay, brain abnormalities, 2/3 syndactyly of the toes, facial dysmorphisms, low total and LDL-cholesterol, and abnormal urine organic acids.
More Infomation

Kanmalar, M., Abdul Sani, S. F., Kamri, N. I. N. B., Said, N. A., Jamil, A. H., Kuppusamy, S., ... & Bradley, D. A. (2022). Raman spectroscopy biochemical characterisation of bladder cancer cisplatin resistance regulated by FDFT1: a review. Cellular & Molecular Biology Letters, 27(1), 1-20.

Pu, X., Lin, X., Qi, Y., Li, Y., Li, T., Liu, Y., & Wei, D. (2022). Effects of Fdft 1 gene silencing and VD3 intervention on lung injury in hypoxia-stressed rats. Genes & Genomics, 44(10), 1201-1213.

Huang, R., Zhang, C., Wang, X., Zou, X., Xiang, Z., Wang, Z., ... & Hu, H. (2022). Identification of FDFT1 as a potential biomarker associated with ferroptosis in ccRCC. Cancer Medicine.

Huang, C., Wen, Q., Chen, J., Zhong, H., Xiang, X., Xiong, J., & Deng, J. (2022). FDFT1/FGFR2 rearrangement: A newly identified anlotinib-sensitive FGFR2 variant in cholangiocarcinoma. Cancer Treatment and Research Communications, 31, 100568.

Dong, X., Zhu, Y., Wang, S., Luo, Y., Lu, S., Nan, F., ... & Sun, X. (2020). Bavachinin inhibits cholesterol synthesis enzyme FDFT1 expression via AKT/mTOR/SREBP-2 pathway. International Immunopharmacology, 88, 106865.

Lu, J., Zhou, Y., Zheng, X., Chen, L., Tuo, X., Chen, H., ... & Zhao, L. (2020). 20 (S)-Rg3 upregulates FDFT1 via reducing miR-4425 to inhibit ovarian cancer progression. Archives of Biochemistry and Biophysics, 693, 108569.

Weng, M. L., Chen, W. K., Chen, X. Y., Lu, H., Sun, Z. R., Yu, Q., ... & Miao, C. H. (2020). Fasting inhibits aerobic glycolysis and proliferation in colorectal cancer via the Fdft1-mediated AKT/mTOR/HIF1α pathway suppression. Nature communications, 11(1), 1-17.

Lin, X., Wang, H., & Pu, X. (2020). Protective mechanism of fdft1 in steroid hormone synthesis pathway in SD rats with acute hypoxic injury. Genes & genomics, 42(11), 1319-1326.

Tüzmen, Ş., Hostetter, G., Watanabe, A., Ekmekçi, C., Carrigan, P. E., Shechter, I., ... & Mousses, S. (2019). Characterization of farnesyl diphosphate farnesyl transferase 1 (FDFT1) expression in cancer. Personalized Medicine, 16(1), 51-65.

Ma, Y. S., Wu, Z. J., Zhang, H. W., Cai, B., Huang, T., Long, H. D., ... & Fu, D. (2019). Dual regulatory mechanisms of expression and mutation involving metabolism-related genes FDFT1 and UQCR5 during CLM. Molecular Therapy-Oncolytics, 14, 172-178.

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

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