ALDH1L1 Antibodies

Structure of ALDH1L1

The protein encoded by the ALDH1L1 gene has a molecular weight of approximately 98.8 kDa. Its size varies slightly among different species due to sequence differences.

This protein is composed of 902 amino acid residues and forms a typical three-dimensional structure of aldehyde dehydrogenase. Its primary structure folds into two main functional domains: the 10-methyltetrahydrofolate dehydrogenase domain at the N-terminus and the aldehyde dehydrogenase domain at the C-terminus. Together, they constitute the complete enzyme active center. The tertiary structure of the protein depends on the assembly of multiple β-sheet segments and α-helices, forming a deep crevice that accommodates the cofactor NADP+ and the substrate folate analogues. The cysteine residue (Cys707) in the active center acts as a crucial nucleophilic catalyst, working in synergy with the glutamic acid residue (Glu399), to catalyze the irreversible demethylation reaction of the folate intermediate, which is a core step connecting the folate cycle and the one-carbon metabolism network.

Fig. 1 Structural Insights into the Domains and Cofactor Binding Sites of ALDH1L1.¹

Key structural properties of ALDH1L1:

• Contains NADP + combined with catalytic domain and aldehyde dehydrogenase domain the dual structure of domain
• Active center by highly conservative catalytic triplet (Cys707, Glu399, etc.)
• Oxidative deformylation of 10-formyl tetrahydrofolate dependent on cofactor NADP+

Functions of ALDH1L1

The core function of the ALDH1L1 protein is to regulate one-carbon unit metabolism. However, it also plays a role in various cellular physiological processes, including cell proliferation regulation and maintenance of redox homeostasis.

The kinetic properties of this enzyme are characterized by a high affinity for the substrate 10-methyltetrahydrofolate. The reaction is irreversible, which ensures the directional nature of the metabolic flow towards nucleotide synthesis. This is in sharp contrast to the reversible serine hydroxymethyltransferase reaction, jointly forming the fine regulation of the one-carbon metabolism network.

Applications of ALDH1L1 and ALDH1L1 Antibody in Literature

1. Rushing, Blake R., et al. "Exploratory metabolomics underscores the folate enzyme ALDH1L1 as a regulator of glycine and methylation reactions." Molecules 27.23 (2022): 8394. https://doi.org/10.3390/molecules27238394

The article indicates that the absence of the ALDH1L1 enzyme significantly alters the metabolic profile of cancer cells, resulting in decreased levels of glycine, S-adenosylmethionine metabolites, and intermediates of the tricarboxylic acid cycle, while increasing the level of nicotinic acid. These changes may provide a proliferation advantage for cancer cells.

2. Krupenko, Sergey A., and David A. Horita. "The role of single-nucleotide polymorphisms in the function of candidate tumor suppressor ALDH1L1." Frontiers in Genetics 10 (2019): 1013. https://doi.org/10.3389/fgene.2019.01013

The article indicates that ALDH1L1 is a key regulatory enzyme in one-carbon metabolism and is often inhibited in cancer, showing a positive correlation with the malignancy of tumors. The frequent non-synonymous SNPs in its coding region affect the enzyme's function and are associated with specific cancer risks. The underlying mechanism remains to be studied.

3. Tsybovsky, Yaroslav, et al. "Structure of putative tumor suppressor ALDH1L1." Communications Biology 5.1 (2022): 3. https://doi.org/10.1038/s42003-021-02963-9

The article indicates that ALDH1L1 is a tri-domain fused tumor suppressor enzyme that transfers the formyl group between different subunits through an intermediate carrier domain. Its tetrameric structure is indispensable for this catalytic process, revealing the versatility of the acyl carrier protein in dynamic enzyme systems.

4. Nemeth, Daniel, et al. "Aldh1l1-Cre/ER T2 is expressed in unintended cell types of the salivary gland, pancreas, and spleen."microPublication Biology 2023 (2023): 10-17912. https://doi.org/10.17912/micropub.biology.000832

The article indicates that the Aldh1l1-Cre/ERT2 mouse model not only expresses Cre recombinase in astrocytes of the central nervous system, but also shows unexpected activity in exocrine glands such as the spleen, salivary glands, and pancreas, which may affect the interpretation of related experimental data.

5. Sasaki, Masato, et al. "One-carbon metabolizing enzyme ALDH1L1 influences mitochondrial metabolism through 5-aminoimidazole-4-carboxamide ribonucleotide accumulation and serine depletion, contributing to tumor suppression." Scientific Reports 13.1 (2023): 13486. https://doi.org/10.1038/s41598-023-38142-5

The article indicates that in hepatocellular carcinoma, low expression of ALDH1L1 consumes 10-fTHF, leading to the accumulation of the purine synthesis intermediate ZMP. Conversely, its high expression reduces ZMP sensitivity and enhances mitochondrial activity, suggesting that ZMP and AMP analogues may effectively treat patients with low ALDH1L1 expression.

Creative Biolabs: ALDH1L1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality ALDH1L1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom ALDH1L1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our ALDH1L1 antibodies, custom preparations, or technical support, contact us at info@creative-biolabs.com.