|Protein Existence Status||Unreviewed: Protein inferred from homology|
|Presence in other biological fluids/tissue/cells||lysosomes of primary myoblasts, primary glial cells, extracelluar fluids and secretory granules of rat endocrine B cells, saliva, urine, serum|
|Protein Function||Stefin family; cystein cathepsin inhibitor; protects neurons against oxidative stress; involved in the defence of tissues against invasion by pathogens; upregulated in septic injury;|
|Biochemical Properties||Monomeric protein with missing intramolecular disulfide bridges or glycosylation; resistant to proteolytic cleavge but the N-terminal is accessible to protease attack; soluble protein; nuclear concentration is higher than cytoplasmic concentration;|
|Significance in milk||Downregulated in mastitis; role in the protection from bacterial infection|
|Additional Comments||Fibrillation is caused by acididc solvants, high temperature, presence of TFE or high ionic strengths|
|Bibliography||1. Matsuoka, Y., Serizawa, A., Yoshioka, T., Yamamura, J., Morita, Y., Kawakami, H., … Kumegawa, M. (2002). Cystatin C in milk basic protein (MBP) and its inhibitory effect on bone resorption in vitro. Bioscience, Biotechnology, and Biochemistry, 66(12), 2531–2536. https://doi.org/10.1271/bbb.66.2531. |
2. Sotiropoulou, G., Anisowicz, A., & Sager, R. (1997). Identification, cloning, and characterization of cystatin M, a novel cysteine proteinase inhibitor, down-regulated in breast cancer. The Journal of Biological Chemistry, 272(2), 903–910. https://doi.org/10.1074/jbc.272.2.903.
3. Ni, J., Abrahamson, M., Zhang, M., Fernandez, M. A., Grubb, A., Su, J., … Gentz, R. (1997). Cystatin E is a novel human cysteine proteinase inhibitor with structural resemblance to family 2 cystatins. The Journal of Biological Chemistry, 272(16), 10853–10858. https://doi.org/10.1074/jbc.272.16.10853.
4. Mudaliar, M., Tassi, R., Thomas, F. C., McNeilly, T. N., Weidt, S. K., McLaughlin, M., … Zadoks, R. N. (2016). Mastitomics, the integrated omics of bovine milk in an experimental model of Streptococcus uberis mastitis: 2. Label-free relative quantitative proteomics. Molecular BioSystems, 12(9), 2748–2761. https://doi.org/10.1039/c6mb00290k.
5. Maher, K., Jerič Kokelj, B., Butinar, M., Mikhaylov, G., Manček-Keber, M., Stoka, V., … Kopitar-Jerala, N. (2014). A role for stefin B (cystatin B) in inflammation and endotoxemia. The Journal of Biological Chemistry, 289(46), 31736–31750. https://doi.org/10.1074/jbc.M114.609396