Recombinant Human SDSL protein
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Recombinant Human SDSL protein is a Human Full Length protein, in the 1 to 329 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
Serine dehydratase-like, Cancerous serine dehydratase, Glutamate racemase, L-serine deaminase, L-serine dehydratase/L-threonine deaminase, L-threonine dehydratase, Serine dehydratase 2, cSDH, SDHL, TDH, SDH 2, SDSL
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SDSL protein (AB113400)
15% SDS-PAGE of SDSL protein : (1) MW ladder, (2) protein loaded 3ug
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
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
The serine dehydratase-like protein contributes to the metabolism of amino acids an essential process for cellular function and energy production. SDSL does not appear to form part of a larger protein complex but works independently in biochemical pathways related to the breakdown of serine. This activity is significant for maintaining amino acid homeostasis within the cell and supporting gluconeogenesis.
Pathways
Amino acid metabolism and gluconeogenesis represent major biological pathways involving SDSL. In the amino acid metabolism pathway SDSL interacts with enzymes like alanine transaminase and aspartate aminotransferase which further process the products of the dehydratase reaction. In gluconeogenesis the pyruvate produced serves as a substrate for enzymes like pyruvate carboxylase illustrating how SDSL indirectly supports glucose synthesis during fasting or low-carbohydrate intake.
Specifications
Form
Liquid
Additional notes
Conventional chromatography techniques (anion exchange followed by gel filtration with 20mM Tris pH 7.5, 2mM EDTA).
General info
Function
Catalyzes the pyridoxal-phosphate-dependent dehydrative deamination of L-threonine and L-serine to ammonia and alpha-ketobutyrate and pyruvate, respectively (PubMed : 16580895, PubMed : 18342636). Also exhibits racemase activity towards L-glutamate and D-glutamate (By similarity).
Sequence similarities
Belongs to the serine/threonine dehydratase family.
Target data
Product promise
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