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Sigma-Aldrich

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

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.

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Denise C Cornelius et al.
PloS one, 15(6), e0234039-e0234039 (2020-06-20)
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
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
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

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