5089
CD14 human
recombinant, expressed in E. coli, 0.5 mg protein/mL
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.75
Productos recomendados
biological source
human
recombinant
expressed in E. coli
description
0.1 mg recombinant human CHD14 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 100 μg
concentration
0.5 mg protein/mL
technique(s)
cell culture | mammalian: suitable
accession no.
NP_000582
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... CD14(929)
Application
Coating a plate well (6 well plate) with this recombinant CD14 protein in a T cell specific medium at 1-10 μg / well can be used as 1) a human T cell / receptor interaction studies in vitro or 2) a breast cancer biomarker for diagnosis application when combined with CD16 antigen.
Use this procedure as a guideline to determine optimal coating conditions for the culture system of choice.
1. Thaw CD14 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).
2. Add appropriate amount of diluted material to culture surface.
3. Incubate at room temperature for approximately 1.5 hours.
4. Aspirate remaining material.
5. Rinse plates carefully with water and avoid scratching bottom surface of plates.
6. 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 CD14 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).
2. Add appropriate amount of diluted material to culture surface.
3. Incubate at room temperature for approximately 1.5 hours.
4. Aspirate remaining material.
5. Rinse plates carefully with water and avoid scratching bottom surface of plates.
6. Plates are ready for use. They may also be stored at 2-8 °C damp or air dried if sterility is maintained.
Sequence
MASMTGGQQMGRGHHHHHHGNLYFQGTTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPEVDNLTLDGNPFLVPGTALPHEGSMN
Preparation Note
The full-length extracellular domain of the human CD14 gene (20-345 aa) was constructed with 29 N-terminal T7/HIS-tag and expressed in E. coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
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Sepsis is characterized by organ dysfunction due to a dysregulated immune response to infection. Currently, no effective treatment for sepsis exists. Platelets are recognized as mediators of the immune response and may be a potential therapeutic target for the treatment
A-L Feng et al.
Clinical and experimental immunology, 164(1), 57-65 (2011-03-03)
Human peripheral blood monocytes are a heterogeneous population, including CD14(+) CD16(-) 'classical' monocytes and CD14(+) CD16(+) 'proinflammatory' monocytes. CD16(+) monocytes are expanded in various inflammatory conditions. However, little is known about the CD14(+) CD16(+) monocytes in patients with breast cancer.
Pengyu Zhang et al.
Naunyn-Schmiedeberg's archives of pharmacology, 391(12), 1411-1420 (2018-08-30)
Label-free cell phenotypic assays were performed to establish a β2-adrenoceptor (β2-AR) target model in A431 cells and a β1-AR target model in transfected HEK293-β1 cells, using known β2-AR and β1-AR agonists and antagonists. A list of natural compounds was screened
R R Schumann et al.
Science (New York, N.Y.), 249(4975), 1429-1431 (1990-09-21)
The primary structure of lipopolysaccharide binding protein (LBP), a trace plasma protein that binds to the lipid A moiety of bacterial lipopolysaccharides (LPSs), was deduced by sequencing cloned complementary DNA. LBP shares sequence identity with another LPS binding protein found
Li Fang et al.
PloS one, 9(7), e101406-e101406 (2014-07-16)
LPS-binding protein (LBP) and its ligand CD14 are located upstream of the signaling pathway for LPS-induced inflammation. Blocking LBP and CD14 binding might prevent LPS-induced inflammation. In previous studies, we obtained a peptide analog (MP12) for the LBP/CD14 binding site
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