Recombinant Human ALDH3A1 Protein, GST-tagged
Cat.No. : | ALDH3A1-445H |
Product Overview : | Human ALDH3A1 full-length ORF ( AAH04370, 1 a.a. - 453 a.a.) recombinant protein with GST-tag at N-terminal. |
- Specification
- Gene Information
- Related Products
Description : | Aldehyde dehydrogenases oxidize various aldehydes to the corresponding acids. They are involved in the detoxification of alcohol-derived acetaldehyde and in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. The enzyme encoded by this gene forms a cytoplasmic homodimer that preferentially oxidizes aromatic and medium-chain (6 carbons or more) saturated and unsaturated aldehyde substrates. It is thought to promote resistance to UV and 4-hydroxy-2-nonenal-induced oxidative damage in the cornea. The gene is located within the Smith-Magenis syndrome region on chromosome 17. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Sep 2008] |
Source : | Wheat Germ |
Species : | Human |
Tag : | GST |
Molecular Mass : | 75.35 kDa |
AA Sequence : | MSKISEAVKRARAAFSSGRTRPLQF RIQQLEALQRLIQEQEQELVGALAA DLHKNEWNAYYEEVVYVLEEIEYMI QKLPEWAADEPVEKTPQTQQDELYI HSEPLGVVLVIGTWNYPFNLTIQPM VGAIAAGNAVVLKPSELSENMASLL ATIIPQYLDKDLYPVINGGVPETTE LLKERFDHILYTGSTGVGKIIMTAA AKHLTPVTLELGGKSPCYVDKNCDL DVACRRIAWGKFMNSGQTCVAPDYI LCDPSIQNQIVEKLKKSLKEFYGED AKKSRDYGRIISARHFQRVMGLIEG QKVAYGGTGDAATRYIAPTILTDGD PQSPVMQEEIFGPVLPIVCVRSLEE AIQFINQREKPLALYMFSSNDKVIK KMIAETSSGGVAANDVIVHITLHSL PFGGVGNSGMGSYHGKKSFETFSHR RSCLVRPLMNDGGLKVRYPPSPAKM TQH |
Applications : | Enzyme-linked Immunoabsorbent Assay; Western Blot (Recombinant protein); Antibody Production; Protein Array |
Notes : | Best use within three months from the date of receipt of this protein. |
Storage : | Store at -80 centigrade. Aliquot to avoid repeated freezing and thawing. |
Storage Buffer : | 50 mM Tris-HCI, 10 mM reduced Glutathione, pH=8.0 in the elution buffer. |
Gene Name : | ALDH3A1 aldehyde dehydrogenase 3 family, member A1 [ Homo sapiens ] |
Official Symbol : | ALDH3A1 |
Synonyms : | ALDH3A1; aldehyde dehydrogenase 3 family, member A1; ALDH3; aldehyde dehydrogenase, dimeric NADP-preferring; aldehyde dehydrogenase; dimeric NADP preferring; stomach aldehyde dehydrogenase; aldehyde dehydrogenase type III; aldehyde dehydrogenase isozyme 3; ALDHIII; MGC10406; |
Gene ID : | 218 |
mRNA Refseq : | NM_000691 |
Protein Refseq : | NP_000682 |
MIM : | 100660 |
UniProt ID : | P30838 |
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◆ Lysates | ||
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (14)
Ask a questionThe ALDH3A1 protein is primarily involved in the metabolism and detoxification of toxic aldehydes that can be generated within cells. It helps convert these harmful aldehydes into less toxic molecules, thereby protecting cells from their damaging effects. Additionally, ALDH3A1 is involved in maintaining the integrity and function of the cornea by generating osmoprotective molecules to defend against environmental stressors.
Several compounds have been identified as inhibitors or activators of ALDH3A1. Some studies have reported that disulfiram, a drug used in the treatment of alcoholism, can act as an inhibitor of ALDH3A1 activity. On the other hand, certain chemicals and drugs, such as 4-hydroxynonenal and retinoic acid, have been shown to stimulate ALDH3A1 expression and activity. However, further research is needed to fully understand the regulation and potential therapeutic modulation of ALDH3A1.
There is limited evidence suggesting that genetic variations or polymorphisms in the ALDH3A1 gene could potentially influence drug metabolism. Since ALDH3A1 participates in the detoxification of aldehydes, which can be generated as a byproduct of drug metabolism, alterations in its activity might affect the clearance or toxicity of certain drugs. However, more research is needed to establish a clear connection between ALDH3A1 variations and drug metabolism or response.
Yes, ALDH3A1 is involved in the cellular response to oxidative stress. It has been shown to play a role in protecting cells from oxidative damage by detoxifying reactive aldehydes, which are generated as a result of oxidative stress. ALDH3A1's activity helps to prevent the accumulation of toxic aldehydes that can cause cellular damage and oxidative stress.
Mutations or variations in the ALDH3A1 gene or protein have been associated with certain ocular disorders. For example, reduced activity of ALDH3A1 has been linked to the development of age-related nuclear cataracts, a common cause of blindness in the elderly. Additionally, alterations in ALDH3A1 expression and function have been observed in other eye conditions, such as dry eye disease and corneal disorders.
ALDH3A1 has been associated with certain types of cancer. Its overexpression has been observed in some cancer tissues, suggesting a potential role in tumor development and progression. However, the exact functions and mechanisms of ALDH3A1 in cancer are not fully understood. Further studies are needed to elucidate its involvement in cancer biology and whether it could serve as a therapeutic target or diagnostic marker.
Yes, the expression of ALDH3A1 can be altered under certain conditions and diseases. For example, oxidative stress, inflammation, and exposure to specific chemicals or toxins can induce the upregulation or downregulation of ALDH3A1 expression. Additionally, studies have shown that the expression of ALDH3A1 can be modulated in certain pathological conditions, such as cancer, neurodegenerative diseases, and metabolic disorders.
The clinical significance and potential therapeutic applications of ALDH3A1 are still being explored. Its involvement in detoxification processes and protection against oxidative stress suggest that targeting ALDH3A1 could have implications in diseases associated with aldehyde toxicity and oxidative damage. Furthermore, its overexpression in certain cancers could potentially be targeted for therapeutic interventions. However, more research is needed to develop specific therapeutic strategies and to fully understand the role of ALDH3A1 in different diseases.
ALDH3A1 is not directly involved in alcohol metabolism. The primary enzyme responsible for alcohol metabolism is alcohol dehydrogenase (ADH) which converts ethanol into acetaldehyde, which is then further metabolized into acetic acid by aldehyde dehydrogenase (ALDH) enzymes such as ALDH1A1 and ALDH2. ALDH3A1 plays a role in the metabolism of other aldehydes in the body but is not directly involved in alcohol metabolism.
Currently, there are no specific treatments or therapies targeting ALDH3A1 protein for ocular disorders or other conditions. However, research in this field is ongoing, and potential approaches to modulate ALDH3A1 activity or mimic its functions may be explored in the future.
ALDH3A1 has been shown to interact with other proteins or molecules in cellular processes. For example, it has been reported to form complexes with other aldehyde dehydrogenase family members, such as ALDH1A1, ALDH2, and ALDH5A1, in the detoxification of aldehydes. ALDH3A1 has also been found to interact with heat shock proteins and corneal proteins, suggesting its involvement in cellular stress response and maintaining corneal integrity.
The ALDH3A1 protein is expressed in various tissues and organs, but it displays higher levels in certain tissues. It is predominantly found in the cornea, where it plays a critical role in corneal integrity and protection against oxidative stress. Additionally, ALDH3A1 is expressed in the liver, lung, skin, and other tissues associated with detoxification and protection against aldehyde-related damage.
The regulation of ALDH3A1 protein expression and activity is influenced by various factors. It can be regulated at the transcriptional level by specific DNA-binding transcription factors that either enhance or repress its gene expression. Additionally, post-translational modifications such as phosphorylation, acetylation, and glycosylation can impact the stability and enzymatic activity of the ALDH3A1 protein.
The measurement of ALDH3A1 protein levels or activity can be done through various laboratory techniques. One common approach is using enzyme activity assays, which involve measuring the rate at which ALDH3A1 converts its specific substrate into a product. Additionally, immunological methods such as Western blotting or immunohistochemistry can be employed to detect and quantify ALDH3A1 protein levels in tissues or biological fluids.
Customer Reviews (3)
Write a reviewIts ease of use and versatility make it an excellent choice for various applications, including ELISA assays and protein electron microscopy structure analysis.
Its exceptional performance and reliable outcomes make it an invaluable asset in advancing scientific understanding and uncovering important biological insights.
I have consistently obtained outstanding results using the ALDH3A1 Protein, which has significantly enhanced the efficiency and reliability of my research.
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