Recombinant Human ASAH1 protein (GST tag N-Terminus)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human ASAH1 protein (GST tag N-Terminus) is a Human Fragment protein, in the 25 to 124 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
View Alternative Names
ASAH, HSD-33, HSD33, ASAH1, Acid ceramidase, AC, ACDase, Acid CDase, Acylsphingosine deacylase, Glycosylceramide deacylase, N-acylethanolamine hydrolase ASAH1, N-acylsphingosine amidohydrolase, Putative 32 kDa heart protein, PHP32
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human ASAH1 protein (GST tag N-Terminus) (AB114948)
12.5% SDS-PAGE showing ab114948 at approximately 36.63kDa.
Stained with Coomassie Blue.
Reactivity data
Product details
Best used within three months from the date of receipt.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ASAH1 influences several important cellular processes by controlling the levels of ceramide and sphingosine. These lipids are not just structural components of membranes; they participate actively in cell signaling. ASAH1 exists as part of a larger complex that includes other enzymes involved in sphingolipid metabolism. Changes in ceramide levels influence apoptosis and cell proliferation indicating ASAH1's role as a regulator in these processes.
Pathways
ASAH1 is central to the sphingolipid metabolism pathway. This pathway is interconnected with the apoptosis signaling pathway. By converting ceramide to sphingosine ASAH1 links the complex ceramide/sphingosine balance affecting cell survival and death decisions. It interacts with other enzymes such as sphingosine kinase 1 and ceramide synthases which further maintain the dynamic regulation between sphingosine and ceramide levels.
Specifications
Form
Liquid
General info
Function
Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (PubMed : 10610716, PubMed : 11451951, PubMed : 15655246, PubMed : 26898341, PubMed : 36752535, PubMed : 7744740, PubMed : 7852294). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed : 10610716). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (PubMed : 15655246, PubMed : 7744740). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed : 12764132, PubMed : 12815059). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (PubMed : 12764132). Also has an N-acylethanolamine hydrolase activity (PubMed : 15655246). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (PubMed : 17713573). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (PubMed : 22261821).. Isoform 2. May directly regulate steroidogenesis by binding the nuclear receptor NR5A1 and negatively regulating its transcriptional activity.
Sequence similarities
Belongs to the acid ceramidase family.
Post-translational modifications
N-glycosylated.. Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond (PubMed:11451951, PubMed:29692406, PubMed:30525581, PubMed:7744740). Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (PubMed:29692406, PubMed:30525581). The beta chain may undergo an additional C-terminal processing (PubMed:12815059).
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com