Code | CSB-YP002682MO |
MSDS | |
Size | Pls inquire |
Source | Yeast |
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Code | CSB-EP002682MO-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-BP002682MO |
MSDS | |
Size | Pls inquire |
Source | Baculovirus |
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Code | CSB-MP002682MO |
MSDS | |
Size | Pls inquire |
Source | Mammalian cell |
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This BGLAP protein is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
BGLAP is a small protein found abundantly in the mineralized extracellular matrix (ECM) of bone, dentin, and cementum [1]. It is produced by osteoblasts and odontoblasts, making it the most abundant non-collagen protein in bone-like tissue [2]. BGLAP was initially identified in bone and has been found to have implications beyond bone health. Studies have shown that BGLAP promotes cell growth and invasion of pancreatic cancer cells [3].
Furthermore, BGLAP is crucial in bone metabolism and mineralization. It is commonly used as a clinical marker of bone turnover, and its absence has been associated with increased trabecular bone and improved biomechanics in animal models [5]. Moreover, the BGLAP gene encodes osteocalcin, which binds to calcium and hydroxyapatite, essential components of bones, thus regulating bone metabolism and calcium ion homeostasis [6].
BGLAP has been reported to modulate osteogenic differentiation of mesenchymal stem cells and influence mineral species maturation [7]. Furthermore, as immature osteoblasts mature, they express ample BGLAP, highlighting its importance in osteoblast differentiation and skeletal homeostasis [8].
References:
[1] P. Giovani, L. Martins, C. Salmon, L. Mofatto, A. Leme, R. Puppin‐Rontaniet al., Comparative proteomic analysis of dental cementum from deciduous and permanent teeth, Journal of Periodontal Research, vol. 56, no. 1, p. 173-185, 2020. https://doi.org/10.1111/jre.12808
[2] Q. Li, H. Zhou, C. Wang, & Z. Zhu, Long non-coding rna linc01133 promotes osteogenic differentiation of human periodontal ligament stem cells via microrna-30c / bone gamma-carboxyglutamate protein axis, Bioengineered, vol. 13, no. 4, p. 9603-9613, 2022. https://doi.org/10.1080/21655979.2022.2054912
[3] H. Kayed, S. Bekasi, S. Keleg, C. Michalski, T. Giese, H. Frießet al., Bglap is expressed in pancreatic cancer cells and increases their growth and invasion, Molecular Cancer, vol. 6, no. 1, 2007. https://doi.org/10.1186/1476-4598-6-83
[4] S. Das, N. Sharma, & S. Elbein, Analysis of osteocalcin as a candidate gene for type 2 diabetes (t2d) and intermediate traits in caucasians and african americans, Disease Markers, vol. 28, no. 5, p. 281-286, 2010. https://doi.org/10.1155/2010/246845
[5] L. Lambert, A. Challa, A. Niu, L. Zhou, J. Tucholski, M. Johnsonet al., Increased trabecular bone and improved biomechanics in an osteocalcin null rat model created by crispr/cas9 technology, Disease Models & Mechanisms, 2016. https://doi.org/10.1242/dmm.025247
[6] M. Semeghini, P. Scalize, M. Coelho, R. Fernandes, D. Pitol, M. Tavareset al., Lycopene prevents bone loss in ovariectomized rats and increases the number of osteocytes and osteoblasts, Journal of Anatomy, vol. 241, no. 3, p. 729-740, 2022. https://doi.org/10.1111/joa.13672
[7] H. Lee, S. Min, Y. Park, & J. Park, The role of insulin-like growth factor-2 on the cellular viability and differentiation to the osteogenic lineage and mineralization of stem cells cultured on deproteinized bovine bone mineral, Applied Sciences, vol. 10, no. 16, p. 5471, 2020. https://doi.org/10.3390/app10165471
[8] L. Wang, H. Yang, J. Huang, S. Pei, L. Wang, J. Fenget al., Targeted ptpn11 deletion in mice reveals the essential role of shp2 in osteoblast differentiation and skeletal homeostasis, Bone Research, vol. 9, no. 1, 2021. https://doi.org/10.1038/s41413-020-00129-7
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