product name
VitroCol®, Collagen from Human neonatal fibroblasts, 97% Type I with the remainder of Type III collagen, suitable for cell culture
质量水平
无菌性
sterile-filtered
形式
lyophilized
包装
pkg of 15 mg
制造商/商品名称
Advanced BioMatrix
技术
cell culture | mammalian: suitable
杂质
<1 EU/mL Endotoxin level
运输
wet ice
储存温度
−20°C
一般描述
VitroCol® collagen is naturally secreted from human neo-natal fibroblast cells. The human fibroblasts are cultured in optimal conditions allowing the fibroblasts to naturally and efficiently secret extracellular matrix. The extracellular matrix is then processed and purified to yield the naturally produced human collagen.
VitroCol® is approximately 97% Type I human collagen with the remainder being comprised of Type III collagen. It contains high monomer content as measured by gel permeation chromatography.
VitroCol® is especially ideal for human cell culture systems when coating of surfaces and providing preparations of thin layers of culturing cells. It is not recommend for the formation of a solid gel. VitroCol® is supplied as a sterile, lyophilized powder.
VitroCol® is approximately 97% Type I human collagen with the remainder being comprised of Type III collagen. It contains high monomer content as measured by gel permeation chromatography.
VitroCol® is especially ideal for human cell culture systems when coating of surfaces and providing preparations of thin layers of culturing cells. It is not recommend for the formation of a solid gel. VitroCol® is supplied as a sterile, lyophilized powder.
制备说明
This product is supplied as a lyophilized powder with 15 mg of human collagen. When reconstituted with 5 ml of sterile 0.01 N HCl, a concentration of approximately 3 mg/ml is achieved.
法律信息
VitroCol is a registered trademark of Advanced BioMatrix, Inc.
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
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Magnetic resonance (MR) spectroscopy has potential to non-invasively detect metabolites of diagnostic significance for precision oncology. Yet, many metabolites have similar chemical shifts, yielding highly convoluted 1H spectra of intact biological material and limiting diagnostic utility. Here, we show that
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