Analytical Data
-
Gene name
pyp
- Application
-
Alternative Names
pyp；BHLHE15；Single-minded homolog 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q15181
-
Expression Region
2-289aa
-
AA Sequence
MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKGKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN
-
Molecular Weight
32.6 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PYRIMIDINE-5'-Nucleotide Phosphorylase (PYP) represents a fascinating subject in protein research due to its essential role in various biochemical pathways, notably in nucleotide metabolism. As a key enzyme catalyzing the reversible phosphorolysis of pyrimidine nucleotides, it plays a significant role in nucleotide salvage pathways, which are critical for cellular energy balance and metabolic regulation. The study of PYP involves understanding its structure-function relationship, as this enzyme exhibits a unique and well-preserved three-dimensional structure across different species. Investigations into PYP's enzymatic mechanisms have significant implications for therapeutic applications, particularly in cancer and metabolic disorders, where nucleotide metabolism is frequently disrupted. Furthermore, the exploration of PYP's activity also extends to the development of biosensors and biocatalytic processes, highlighting its potential in biotechnology. Given the growing interest in metabolic engineering, PYP serves as a model for studying enzymatic specificity and efficiency, making it an invaluable component of metabolic pathway elucidation and manipulation in both basic and applied research. As scientists continue to unravel the complexities surrounding PYP, this enzyme offers insights not only into fundamental metabolic processes but also into the broader implications of metabolic regulation in health and disease.
