Code | CSB-YP001561BO |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP001561BO-B |
MSDS | |
Size | Pls inquire |
Source | E.coli |
Conjugate | Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag. |
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Code | CSB-MP001561BO |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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Albumin (ALB) stands as the predominant plasma protein, pivotal in diverse physiological processes [1]. It serves as a carrier protein, facilitating the transport and delivery of essential molecules like metabolites and fatty acids throughout the body [1]. In addition, albumin regulates blood osmotic pressure, crucial for maintaining proper fluid balance in the circulatory system [1]. Its multifunctional role underscores its significance in critical physiological functions [2]. In the healing process, its 66-kDa protein form plays a notable role [3]. Moreover, albumin participates in the transport of free fatty acids, particularly long-chain fatty acids, crucial for lipid metabolism [4][5]. The developmentally regulated presence of albumin in the brain hints at its potential importance in neural cell differentiation [6][7]. Furthermore, albumin acts as a signaling molecule modulating cell function, implicating its involvement in cellular signaling pathways [8]. Structural and immunologic characterization of albumins across species offers insights into their similarities and differences, revealing evolutionary aspects of albumin function [9].
References:
[1] L. Jerković, A. Voegele, S. Chwatal, F. Kronenberg, C. Radcliffe, M. Wormaldet al., "Afamin is a novel human vitamin e-binding glycoprotein characterization and in vitro expression", Journal of Proteome Research, vol. 4, no. 3, p. 889-899, 2005. https://doi.org/10.1021/pr0500105
[2] M. Berezin, H. Lee, W. Akers, G. Nikiforovich, & S. Achilefu, "Ratiometric analysis of fluorescence lifetime for probing binding sites in albumin with near‐infrared fluorescent molecular probes", Photochemistry and Photobiology, vol. 83, no. 6, p. 1371-1378, 2007. https://doi.org/10.1111/j.1751-1097.2007.00173.x
[3] M. Yadav, A. Singh, S. Ali, N. Rizivi, S. Hussain, & V. Kumar, "Role of serum albumin in fracture healing", International Journal of Biomedical Research, vol. 6, no. 7, p. 452, 2015. https://doi.org/10.7439/ijbr.v6i7.2259
[4] B. Rogers, D. Dong, Z. Li, & Z. Li, "Recombinant human serum albumin fusion proteins and novel applications in drug delivery and therapy", Current Pharmaceutical Design, vol. 21, no. 14, p. 1899-1907, 2015. https://doi.org/10.2174/1381612821666150302120047
[5] W. Davidson, V. Birt, T. Birt, & J. Green, "Palmitate‐binding, serum albumin‐like proteins in salmonids", Febs Letters, vol. 233, no. 2, p. 299-302, 1988. https://doi.org/10.1016/0014-5793(88)80446-0
[6] A. Tabernero, E. Lavado, B. Granda, A. Velasco, & J. Medina, "Neuronal differentiation is triggered by oleic acid synthesized and released by astrocytes", Journal of Neurochemistry, vol. 79, no. 3, p. 606-616, 2001. https://doi.org/10.1046/j.1471-4159.2001.00598.x
[7] A. Tabernero, A. Velasco, B. Granda, E. Lavado, & J. Medina, "Transcytosis of albumin in astrocytes activates the sterol regulatory element-binding protein-1, which promotes the synthesis of the neurotrophic factor oleic acid", Journal of Biological Chemistry, vol. 277, no. 6, p. 4240-4246, 2002. https://doi.org/10.1074/jbc.m108760200
[8] T. Weber, S. Negash, S. Heather, K. Ramos, B. Thrall, & T. Squier, "Calmodulin involvement in stress-activated nuclear localization of albumin in jb6 epithelial cells", Biochemistry, vol. 43, no. 23, p. 7443-7450, 2004. https://doi.org/10.1021/bi049731s
[9] K. Majorek, P. Porebski, A. Dayal, M. Zimmerman, K. Jablonska, A. Stewartet al., "Structural and immunologic characterization of bovine, horse, and rabbit serum albumins", Molecular Immunology, vol. 52, no. 3-4, p. 174-182, 2012. https://doi.org/10.1016/j.molimm.2012.05.011
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DTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA