An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most abundant cellular protein in terms of copy number, there can be up to one million Lpp molecules per cell. About one-third of Lpp is bound to the PGN (called bound or periplasmic) the rest is called free or transmembrane. The 'free' form can be surface labeled by membrane impermeable agents and so must cross the outer membrane; it is thought that this transmembrane form is still anchored in the inner leaflet of the outer membrane. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable). The role of the cell surface-exposed, free form (transmembrane) of Lpp is unknown.
规格 | 价格/CNY | 货期 | 数量 | |
---|---|---|---|---|
20 μg | ¥ 2,290 | 20日内发货 | ||
100 μg | ¥ 4,320 | 20日内发货 | ||
1 mg | ¥ 14,600 | 20日内发货 |
产品描述 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most abundant cellular protein in terms of copy number, there can be up to one million Lpp molecules per cell. About one-third of Lpp is bound to the PGN (called bound or periplasmic) the rest is called free or transmembrane. The 'free' form can be surface labeled by membrane impermeable agents and so must cross the outer membrane; it is thought that this transmembrane form is still anchored in the inner leaflet of the outer membrane. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable). The role of the cell surface-exposed, free form (transmembrane) of Lpp is unknown. |
种属 | E. coli |
表达系统 | E. coli |
标签 | N-terminal 6xHis-KSI-tagged |
蛋白编号 | P69776 |
氨基酸序列 | CSSNAKIDQLSSDVQTLNAKVDQLSNDVNAMRSDVQAAKDDAARANQRLDNMATKYRK Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
蛋白构建 | 21-78 aa |
蛋白纯度 | > 85% as determined by SDS-PAGE. |
分子量 | 21.8 kDa (predicted) |
缓冲液 | Tris-based buffer,50% glycerol |
复溶方法 | A hardcopy of COA with reconstitution instructions is sent along with the products. Please refer to it for detailed information. |
存储 |
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. |
运输方式 |
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. |
研究背景 | An outer membrane lipoprotein that controls the distance between the inner and outer membranes; adding residues to Lpp increases the width of the periplasm. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to the maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. The most abundant cellular protein in terms of copy number, there can be up to one million Lpp molecules per cell. About one-third of Lpp is bound to the PGN (called bound or periplasmic) the rest is called free or transmembrane. The 'free' form can be surface labeled by membrane impermeable agents and so must cross the outer membrane; it is thought that this transmembrane form is still anchored in the inner leaflet of the outer membrane. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable). The role of the cell surface-exposed, free form (transmembrane) of Lpp is unknown. |
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recombinant recombinant-proteins proteins protein