Recombinant Full Length Human ALDH4A1 Protein, GST-tagged
Cat.No. : | ALDH4A1-1410HF |
Product Overview : | Human ALDH4A1 full-length ORF ( AAH07581, 1 a.a. - 563 a.a.) recombinant protein with GST-tag at N-terminal. |
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Description : | This protein belongs to the aldehyde dehydrogenase family of proteins. This enzyme is a mitochondrial matrix NAD-dependent dehydrogenase which catalyzes the second step of the proline degradation pathway, converting pyrroline-5-carboxylate to glutamate. Deficiency of this enzyme is associated with type II hyperprolinemia, an autosomal recessive disorder characterized by accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. [provided by RefSeq, Jun 2009] |
Source : | In Vitro Cell Free System |
Species : | Human |
Tag : | GST |
Molecular Mass : | 87.67 kDa |
Protein Length : | 563 amino acids |
AA Sequence : | MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL QKALKDLKGR MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS LLNKAIEAAL AARKEWDLKP IADRAQIFLK AADMLSGPRR AEILAKTMVG QGKTVIQAEI DAAAELIDFF RFNAKYAVEL EGQQPISVPP STNSTVYRGL EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML ASYAVYRILR EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA CSRLYVPHSL WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI KKWLEHARSS PSLTILAGGK CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG PVLSVYVYPD DKYKETLQLI DSTTSYGLTG AVFSQDKDVV QEATKVLRNA AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR WTSPQVIKET HKPLGDWSYA YMQ |
Applications : | Enzyme-linked Immunoabsorbent Assay; Western Blot (Recombinant protein); Antibody Production; Protein Array |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Storage Buffer : | 50 mM Tris-HCl, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Gene Name : | ALDH4A1 aldehyde dehydrogenase 4 family, member A1 [ Homo sapiens ] |
Official Symbol : | ALDH4A1 |
Synonyms : | ALDH4A1; aldehyde dehydrogenase 4 family, member A1; ALDH4; delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5CDh; P5C dehydrogenase; aldehyde dehydrogenase family 4 member A1; mitochondrial delta-1-pyrroline 5-carboxylate dehydrogenase; P5CD; DKFZp779M035 |
Gene ID : | 8659 |
mRNA Refseq : | NM_001161504 |
Protein Refseq : | NP_001154976 |
MIM : | 606811 |
UniProt ID : | P30038 |
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Q&As (14)
Ask a questionThe impact of ALDH4A1 gene variations on an individual's response to medications has not been extensively studied. However, since ALDH4A1 is involved in proline metabolism, it is possible that certain variations in this gene may influence the metabolism or efficacy of medications that are metabolized by proline-related pathways. Further research is needed to explore this potential association.
Mutations in the ALDH4A1 gene can cause a rare autosomal recessive disorder called hyperprolinemia type II or pyrroline-5-carboxylate reductase 1 deficiency. This condition is characterized by elevated levels of proline and P5C in the body, and it may lead to intellectual disability, developmental delay, seizures, and other neurological symptoms.
Currently, there are no specific drugs or therapies that directly target ALDH4A1. However, ALDH inhibitors, such as disulfiram, have been investigated for their potential to inhibit multiple ALDH enzymes, including ALDH4A1. These inhibitors have shown promise in preclinical studies for various diseases, including cancer and neurodegenerative disorders. Further research is necessary to explore the therapeutic potential of targeting ALDH4A1 specifically.
There is limited research on the impact of ALDH4A1 gene variations on disease susceptibility. However, a few studies have suggested that certain variations in the ALDH4A1 gene may be associated with an increased risk of developing Alzheimer's disease and schizophrenia. Further research is needed to confirm these findings and understand the underlying mechanisms.
As of now, there is limited information on ongoing clinical trials specifically investigating ALDH4A1. However, there may be studies related to ALDH enzymes or metabolic pathways that indirectly involve ALDH4A1. It is recommended to search clinical trial databases or consult with healthcare professionals for the most up-to-date information on ongoing research related to ALDH4A1 and its potential implications in disease.
Apart from its role in proline catabolism, ALDH4A1 has been found to interact with other proteins and participate in various metabolic pathways. It is involved in the synthesis of polyamines, which are important for cell growth and proliferation. Additionally, ALDH4A1 has been associated with the regulation of reactive oxygen species (ROS) levels in cells, suggesting a potential role in oxidative stress response.
While the direct link between ALDH4A1 and collagen production is not well-established, there is some evidence suggesting an indirect connection. Proline, which is produced through the action of ALDH4A1, is an essential amino acid required for collagen synthesis. Therefore, disturbances in proline metabolism, such as in ALDH4A1 deficiency, may potentially impact collagen production and affect connective tissues' integrity.
The regulation of ALDH4A1 protein levels and activity is not fully understood. However, studies suggest that its expression can be influenced by various factors, including cellular stress, oxidative conditions, and transcriptional regulation. For example, studies have shown that the ALDH4A1 gene can be upregulated under conditions of oxidative stress. Further research is needed to elucidate the precise mechanisms involved in the regulation of ALDH4A1 in the body.
Yes, the ALDH4A1 protein is expressed in various tissues and organs. It is known to be present in high levels in the liver, kidney, and brain. It is also found in lower amounts in other tissues such as muscle, heart, and lung.
The role of ALDH4A1 in cancer is not well-studied, and its involvement in cancer development or progression is not clearly understood. However, there is some emerging evidence suggesting a potential link between ALDH4A1 and certain forms of cancer, such as breast cancer and lung adenocarcinoma. Future research is needed to further investigate the significance of ALDH4A1 in cancer biology.
Yes, ALDH4A1 deficiency, also known as pyrroline-5-carboxylate dehydrogenase deficiency, is a rare genetic disorder caused by mutations in the ALDH4A1 gene. This condition leads to impaired proline metabolism and elevated levels of P5C and proline in the body. ALDH4A1 deficiency can result in a range of neurological symptoms, including developmental delay, seizures, intellectual disability, and behavioral abnormalities.
Currently, there are no known drugs or compounds specifically targeted towards modulating the expression or activity of ALDH4A1. However, research in this area is ongoing, and future studies may shed light on potential therapeutics that can influence the activity of this enzyme.
ALDH4A1 is not directly involved in alcohol metabolism. Alcohol metabolism primarily involves the activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) enzymes. ALDH4A1 is part of a different metabolic pathway involved in proline breakdown, and its function is unrelated to alcohol metabolism.
The activity of the ALDH4A1 protein can be regulated through several mechanisms. One such mechanism involves the feedback inhibition by its product, glutamate. Elevated levels of glutamate can inhibit ALDH4A1 activity to prevent unnecessary production of glutamate. Additionally, post-translational modifications or the presence of specific co-factors may also impact the activity of ALDH4A1.
Customer Reviews (3)
Write a reviewIts versatility allows for exploring its various roles and functions, shedding light on its significance in crucial biochemical pathways and cellular processes.
By incorporating the ALDH4A1 Protein into their studies, scientists have the opportunity to conduct their research with utmost confidence, paving the way for groundbreaking discoveries and novel insights in their respective fields.
Considering the aforementioned qualities, I wholeheartedly recommend the ALDH4A1 Protein to fellow researchers in search of a top-tier protein solution that not only meets their experimental needs but also benefits from exceptional technical support.
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