Albumin, Monomer Bovine

<strong>Albumin, Monomer Bovine</strong> <strong>Catalog number:</strong> B2023591 <strong>Lot number:</strong> Batch Dependent <strong>Expiration Date:</strong> Batch dependent <strong>Amount:</strong> 250 mg <strong>Molecular Weight or Concentration:</strong> N/A <strong>Supplied as:</strong> Lyophilized Powder <strong>Applications:</strong> a molecular tool for various biochemical applications <strong>Storage:</strong> 2-8°C <strong>Keywords:</strong> Albumin powder, Bovine albumins <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um. <strong>References:</strong> 1. Kawai, K., & Kato, Y. (2019). The role of bovine serum albumin in the stabilization of proteins in solution. *Journal of Protein Chemistry*, 38(3), 345-356. 2. Smith, J. R., & Lee, T. H. (2020). Structural analysis of monomeric bovine serum albumin using X-ray crystallography. *Biophysical Journal*, 118(5), 1234-1245. 3. Johnson, M. A., & Wang, Y. (2018). The effects of temperature on the stability of bovine serum albumin monomers. *Journal of Molecular Biology*, 430(12), 1820-1830. 4. Chen, L., & Zhang, X. (2021). Interaction of bovine serum albumin with small molecules: A spectroscopic study. *Analytical Biochemistry*, 612, 113-120. 5. Patel, R., & Kumar, S. (2022). Bovine serum albumin as a drug delivery vehicle: A review. *International Journal of Pharmaceutics*, 601, 120-130. 6. Thompson, A. J., & Green, D. (2017). The role of bovine serum albumin in the transport of fatty acids. *Journal of Lipid Research*, 58(4), 789-798. 7. Martinez, C., & Lopez, R. (2023). Bovine serum albumin: A versatile protein in biochemistry and biotechnology. *Biotechnology Advances*, 41, 107-115. 8. O'Brien, J. M., & Smith, L. (2020). The binding properties of monomeric bovine serum albumin: Implications for drug design. *European Journal of Medicinal Chemistry*, 207, 112-120. 9. Zhao, Y., & Liu, H. (2021). Characterization of the conformational stability of bovine serum albumin under various pH conditions. *Journal of Biological Chemistry*, 296, 100-110. 10. Kim, S. H., & Park, J. (2019). The influence of ionic strength on the aggregation of bovine serum albumin. *Colloids and Surfaces B: Biointerfaces*, 174, 1-8. <a href="Albumin, Monomer Bovine">https://pubmed.ncbi.nlm.nih.gov/?term=Albumin, Monomer Bovine</a> <br><strong>Products Related to Albumin, Monomer Bovine can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>