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5096

Sigma-Aldrich

CD86 human

recombinant, expressed in E. coli, 0.5 mg protein/mL

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.75

biological source

human

recombinant

expressed in E. coli

description

0.1 mg recombinant human CD86 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

accession no.

NP_008820

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CD86(942)

Application

Coating a plate well (6 well plate) with this recombinant CD86 protein in T cell specific medium at 1-10 μg/well allows for use as 1) a coating matrix protein for human T cell/ receptor interaction or as a highly purified recombinant antigen or 2) as a culture matrix protein for T cell differentiation regulation studies in vitro.

Use this procedure as a guideline to determine optimal coating conditions for the culture system of choice.
1. Thaw CD86 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

MASMTGGQQMGRGHHHHHHGNLYFQGGEFELPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGIMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIP

Preparation Note

The full-length extracellular domain of the human CD86 gene (24 - 247 aa, Isoform-2) was constructed with 31 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 as soluble protein.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Valentine V Courouble et al.
Journal of the American Society for Mass Spectrometry, 32(7), 1618-1630 (2021-06-15)
Coronavirus (CoV) nonstructural proteins (nsps) assemble to form the replication-transcription complex (RTC) responsible for viral RNA synthesis. nsp7 and nsp8 are important cofactors of the RTC, as they interact and regulate the activity of RNA-dependent RNA polymerase and other nsps.
Emmanuelle Benard et al.
Frontiers in immunology, 9, 2085-2085 (2018-10-04)
We created APC-mimetic synthetic substrates to study the impact of ligand clustering on T cell activation and spreading. The substrates exhibit antibodies directed against the TCR-complex in the form of a patterned array of sub micrometric dots surrounded by a
Valentine V Courouble et al.
bioRxiv : the preprint server for biology (2021-03-11)
Coronavirus (CoV) non-structural proteins (nsps) assemble to form the replication-transcription complex (RTC) responsible for viral RNA synthesis. nsp7 and nsp8 are important cofactors of the RTC, as they interact and regulate the activity of RNA-dependent RNA polymerase (RdRp) and other
Ruchi Yadav et al.
Science advances, 8(49), eadd2191-eadd2191 (2022-12-10)
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic. Its genome is translated into two large polyproteins subsequently cleaved by viral papain-like protease and main protease (Mpro). Polyprotein processing is essential yet incompletely understood. We studied Mpro-mediated
Xiao-Nan Zhang et al.
Chemical science, 13(7), 1982-1991 (2022-03-22)
Among various protein posttranslational modifiers, poly-ADP-ribose polymerase 1 (PARP1) is a key player for regulating numerous cellular processes and events through enzymatic attachments of target proteins with ADP-ribose units donated by nicotinamide adenine dinucleotide (NAD+). Human PARP1 is involved in

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