Well-designed Pd-L1 Tumor Immunotherapy - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM
Well-designed Pd-L1 Tumor Immunotherapy - (2S,3R)-2-Amino-3-hydroxybutanoic acid Cas: 72-19-5 99% White crystalline powder – XD BIOCHEM Detail:
| Catalog Number | XD90285 |
| Product Name | (2S,3R)-2-Amino-3-hydroxybutanoic acid |
|
CAS |
72-19-5 |
|
Molecular Formula |
C4H9NO3 |
|
Molecular Weight |
119.11916 |
| Storage Details | Ambient |
|
Harmonized Tariff Code |
29225000 |
Product Specification
| Assay | 99 – 101% |
| Appearance | White crystalline powder |
| Specific rotation | -27.5 to -29.0 |
| Heavy metals | 10ppm Max. |
| AS | 10ppm max |
| pH | 5.2 – 6.5 |
| SO4 | <0.020% |
| Fe | 10ppm max |
| Loss on Drying | <0.20% |
| Residue on Ignition | <0.10% |
| Transmittance | NLT 98% |
| Cl | <0.02% |
| Ammonium salt | <0.02% |
Serine/threonine protein phosphatases have been described in many pathogenic bacteria as essential enzymes involved in phosphorylation-dependent signal transduction pathways and frequently associated with the virulence of these organisms. An inspection of Mycoplasma synoviae genome revealed the presence of a gene (prpC) encoding a putative protein phosphatase of the protein phosphatase 2C (PP2C) subfamily. Here, we report a complete biochemical characterization of M. synoviae phosphatase (PrpC) and the particular role of metal ions in the structure-function relationship of this enzyme. PrpC amino acid sequence analysis revealed that all the residues involved in the dinuclear metal center and the putative third metal ion-coordinating residues, conserved in PP2C phosphatases, are present in PrpC. PrpC is a monomeric protein able to dephosphorylate phospho-substrates with Mn(2+) ions’ dependence. Thermal stability analysis demonstrated the enzyme stability at mild temperatures and the inf luence of Mn(2+) ions in this property. Mass spectrometry analysis suggested that three metal ions bind to PrpC, two of which with an apparent high-affinity constant. Mutational analysis of the putative third metal-coordinating residues, Asp122 and Arg164, revealed that these variants exhibited a weaker binding of manganese ions, and that both mutations affected PrpC phosphatase activity. According to these results, PrpC is a metal-dependent protein phosphatase member with an improved stability in the holo form and with Asp122, possibly implicated in the third metal-binding site, essential to catalytic activity.
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By Doris from New Zealand - 2018.09.21 11:01
The factory can meet continuously developing economic and market needs, so that their products are widely recognized and trusted, and that's why we chose this company.
By Bruno Cabrera from Malta - 2018.02.04 14:13
