Recombinant Human ALDH1A2 protein (His-DHFR)
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Recombinant Human ALDH1A2 protein (His-DHFR) is a Human Fragment protein, in the 210 to 465 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
RALDH2, ALDH1A2, Retinal dehydrogenase 2, RALDH 2, RalDH2, Aldehyde dehydrogenase family 1 member A2, Retinaldehyde-specific dehydrogenase type 2, RALDH(II)
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ALDH1A2 is essential in embryonic development and tissue differentiation. It acts by regulating the levels of retinoic acid necessary for directing gene expression. ALDH1A2 activity is not known to be part of a complex but interacts with other retinoid-binding proteins to achieve its functions. It orchestrates cellular processes by modulating growth factors that are sensitive to retinoic acid.
Pathways
ALDH1A2 is a participant in the retinol metabolism pathway and the broader RA-signaling pathway. It ensures the generation of retinoic acid critical for gene regulation within these pathways. RALDH2's activity is closely related to other dehydrogenases and aldehyde oxidases that contribute to retinoid homeostasis. The interplay with these proteins emphasizes its role in ensuring a balanced retinoic acid supply.
Specifications
Form
Lyophilized
Additional notes
Purified via His tag
General info
Function
Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (PubMed : 29240402, PubMed : 33565183). Retinoate signaling is critical for the transcriptional control of many genes, for instance it is crucial for initiation of meiosis in both male and female (Probable) (PubMed : 33565183). Recognizes retinal as substrate, both in its free form and when bound to cellular retinol-binding protein (By similarity). Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal (By similarity). Displays complete lack of activity with citral (By similarity).
Sequence similarities
Belongs to the aldehyde dehydrogenase family.
Target data
Product promise
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