Recombinant Marinomonas sp. Phosphoserine aminotransferase (serC)

Shipped with Ice Packs
In Stock

Product Specs

Form
Lyophilized powder. We will preferentially ship the format we have in stock. If you have special format requirements, please note them when ordering, and we will fulfill your request.
Lead Time
Delivery time varies based on purchasing method and location. Please consult your local distributor for specific delivery times. All proteins are shipped with standard blue ice packs. For dry ice shipping, please contact us in advance; additional charges will apply.
Notes
Avoid repeated freezing and thawing. Working aliquots are stable at 4°C for up to one week.
Reconstitution
Briefly centrifuge the vial before opening to collect contents at the bottom. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. Adding 5-50% glycerol (final concentration) is recommended for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50% for your reference.
Shelf Life
Shelf life depends on several factors including storage conditions, buffer components, storage temperature, and protein stability. Generally, the liquid form has a shelf life of 6 months at -20°C/-80°C, while the lyophilized form has a shelf life of 12 months at -20°C/-80°C.
Storage Condition
Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
The tag type will be determined during the manufacturing process. If you require a specific tag type, please inform us, and we will prioritize developing it.
Synonyms
serC; Mmwyl1_2859; Phosphoserine aminotransferase; EC 2.6.1.52; Phosphohydroxythreonine aminotransferase; PSAT
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
1-359
Protein Length
full length protein
Purity
>85% (SDS-PAGE)
Species
Marinomonas sp. (strain MWYL1)
Target Names
serC
Target Protein Sequence
MSRVYNFCSG PAALPEAVLK KAQAELLDWH GAGVSVMEMS HRSSEFMSIL ASAKARLSRL MNISDDYEIL FVQGGASTLF SQIPANLANG FESACFLDTG AWSSKAIKEA KKYTKVNVVG SSKAQNYTTV PDFSTLELDE SAAYLHICPN ETIGGLEFAD LPETNLPIVA DLSSTILSRK VDVSKYGVIY AGAQKNVGPA GVVICIIRKD LLARSSDDLP AIWNFAHLAE NDSMINTPPT FAIYLADLVF EWLEAQGGVE AIEQINIRKA QALYDFIDSS NFYSNPVDPV YRSRMNVPFI LADESLEALF LQESEAAGLR TLAGHRSVGG MRASIYNAMP MEGIEALIEF MRGFEERHG
Uniprot No.

Target Background

Function
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Database Links
Protein Families
Class-V pyridoxal-phosphate-dependent aminotransferase family, SerC subfamily
Subcellular Location
Cytoplasm.

Q&A

Data Analysis for Enzyme Activity

  • Q: What methods are used to analyze data from enzyme activity assays for recombinant phosphoserine aminotransferase?

  • A: Data analysis involves calculating kinetic parameters such as Vmax (maximum velocity) and Km (Michaelis constant) using software like GraphPad Prism or similar tools. This helps in understanding the enzyme's efficiency and substrate affinity.

Addressing Data Contradictions

  • Q: How do researchers address contradictions in data from different experiments involving recombinant phosphoserine aminotransferase?

  • A: Contradictions can arise from variations in experimental conditions or sample preparation. Researchers often re-evaluate their methods, ensure consistency in conditions, and consider additional factors like enzyme stability or substrate purity.

Advanced Research Questions: Structural Analysis

  • Q: What advanced techniques are used to study the structural properties of recombinant phosphoserine aminotransferase?

  • A: Techniques such as X-ray crystallography, NMR spectroscopy, and molecular dynamics simulations are employed to understand the enzyme's structure and how it interacts with substrates. This information can guide mutagenesis studies to enhance enzyme activity or specificity.

Methodological Considerations for Mutagenesis Studies

  • Q: How do researchers design mutagenesis studies to improve the activity of recombinant phosphoserine aminotransferase?

  • A: Researchers use site-directed mutagenesis to introduce targeted mutations into the enzyme's gene. They then assess the impact of these mutations on enzyme activity and stability. Computational tools like molecular modeling software can predict potential beneficial mutations.

Comparative Analysis with Other Enzymes

  • Q: How do researchers compare the activity and efficiency of recombinant phosphoserine aminotransferase with other related enzymes?

  • A: Comparative studies involve measuring kinetic parameters (e.g., Vmax, Km) and assessing substrate specificity across different enzymes. This helps in identifying enzymes with superior characteristics for specific applications.

Stable Isotope Probing (SIP) for Environmental Studies

  • Q: How might stable isotope probing (SIP) be applied to study the role of phosphoserine aminotransferase in environmental microbial communities?

  • A: SIP involves labeling substrates with stable isotopes and tracking their incorporation into microbial biomass. This technique can help identify active microbes involved in specific metabolic pathways, including those related to phosphoserine metabolism, in complex environmental samples.

Advanced Techniques for Gene Expression Analysis

  • Q: What advanced techniques are used to analyze gene expression levels of phosphoserine aminotransferase in different conditions?

  • A: Techniques such as quantitative reverse transcription PCR (qRT-PCR) and RNA sequencing (RNA-seq) are used to quantify gene expression levels under various conditions, providing insights into how environmental factors influence enzyme production.

Integration with Metagenomics

  • Q: How can metagenomics be integrated with studies of recombinant phosphoserine aminotransferase to understand its ecological role?

  • A: Metagenomics involves sequencing DNA from environmental samples to identify microbial communities and their functional genes. By combining metagenomics with studies of recombinant enzymes, researchers can link specific genes (like those encoding phosphoserine aminotransferase) to their ecological functions and potential applications.

Data Table Example: Enzyme Activity Assay Results

Enzyme VariantSubstrateVmax (μmol/min)Km (mM)
Wild-TypePhosphoserine10.20.5
Mutant 1Phosphoserine12.50.3
Mutant 2Phosphoserine8.50.7

This table illustrates how different enzyme variants might be compared based on their kinetic parameters.

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