5100
CD164 human
recombinant, expressed in E. coli, 0.5 mg protein/mL
조직 및 계약 가격을 보려면 로그인를 클릭합니다.
크기 선택
보기 변경
제품정보 (DICE 배송 시 비용 별도)
NACRES:
NA.75
UNSPSC Code:
12352200
Form:
liquid
Assay:
≥90% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
biological source
human
recombinant
expressed in E. coli
description
0.05 mg of recombinant human CD164 in 20 mM Tris-HCl buffer, containing NaCl, KCl, EDTA, L-arginine, DTT and glycerol.
sterility
Filtered sterilized solution
assay
≥90% (SDS-PAGE)
form
liquid
packaging
pkg of 50 μg
concentration
0.5 mg protein/mL
accession no.
NP_006007
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... CD164(8763)
Application
Coating a plate well (6 well plate) with this recombinant CD164 matrix protein in HSC cell specific medium at 1-10 μg/well allows for human HSC / receptor interaction studies in vitro.
Use this procedure as a guideline to determine optimal coating conditions for the culture system of choice.
1. Thaw CD164 and dilute to desired concentration using serum-free medium or PBS. The final solution should be sufficiently dilute so the volume added covers the surface evenly (1-10 μg/well, 6 well plate).
Note: Use 1 ml PBS per well in a 6-well plate.
2. Add 1 - 10 μg protein to each well and incubate at 2 to 10 °C overnight.
3. After incubation, aspirate remaining material.
4. Plates are ready for use. They may also be stored at 2-8 °C damp or air dried if sterility is maintained
Use this procedure as a guideline to determine optimal coating conditions for the culture system of choice.
1. Thaw CD164 and dilute to desired concentration using serum-free medium or PBS. The final solution should be sufficiently dilute so the volume added covers the surface evenly (1-10 μg/well, 6 well plate).
Note: Use 1 ml PBS per well in a 6-well plate.
2. Add 1 - 10 μg protein to each well and incubate at 2 to 10 °C overnight.
3. After incubation, aspirate remaining material.
4. Plates are ready for use. They may also be stored at 2-8 °C damp or air dried if sterility is maintained
Preparation Note
The full-length extracellular domain of the human CD164 cDNA (24 - 162 aa) was constructed with 29 N-terminal T7/HIS-tag and expressed in E. coli as inclusion bodies. The final product was refolded using a unique “temperature shift inclusion body refolding” technology and chromatographically purified as soluble protein.
Other Notes
MASMTGGQQMGRGHHHHHHGNLYFQGGEFDKNTTQHPNVTTLAPISNVTSAPVTSLPLVTTPAPETCEGRNSCVSCFNVSVVNTTCFWIECKDESYCSHNSTVSDCQVGNTTDFCSVSTATPVPTANSTAKPTVQPSPSTTSKTVTTSGTTNNTVTPTSQPVRKSTFD
저장 등급
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Benedikt Demmert et al.
Materials (Basel, Switzerland), 12(11) (2019-06-07)
Calcareous biominerals typically feature a hybrid nanogranular structure consisting of calcium carbonate nanograins coated with organic matrices. This nanogranular organisation has a beneficial effect on the functionality of these bioceramics. In this feasibility study, we successfully employed a flow-chemistry approach
Santosh Prasad Gupta et al.
Journal of physics. Condensed matter : an Institute of Physics journal, 32(19), 194004-194004 (2020-01-21)
We present studies on the structure of complexes of the cationic, bilayer-forming surfactant, didodecyldimethylammonium bromide (DDAB), and the anionic polyelectrolyte sodium polyacrylate (PAANa). In the presence of uncomplexed polyelectrolyte in the coexisting aqueous solution, these complexes are found to exhibit
Y Masuzawa et al.
Journal of biochemistry, 112(5), 609-615 (1992-11-01)
The peanut agglutinin (PNA)-binding site is protein-bound Gal beta 1-->3GalNAc, and is a tumor-associated carbohydrate marker expressed in many human carcinomas. PNA-binding glycoproteins isolated from KATO-III human gastric carcinoma cells were deglycosylated by trifluoromethanesulfonic acid, and rabbit antibodies against the