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AB276266

Recombinant human DcR1 protein (His tag)

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(1 Publication)

Recombinant human DcR1 protein (His tag) is a Human Fragment protein, in the 1 to 235 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.

View Alternative Names

CD263, DCR1, LIT, TRAILR3, TRID, UNQ321/PRO366, TNFRSF10C, Tumor necrosis factor receptor superfamily member 10C, Antagonist decoy receptor for TRAIL/Apo-2L, Decoy TRAIL receptor without death domain, Decoy receptor 1, Lymphocyte inhibitor of TRAIL, TNF-related apoptosis-inducing ligand receptor 3, TRAIL receptor without an intracellular domain, DcR1, TRAIL receptor 3, TRAIL-R3

2 Images
Functional Studies - Recombinant human DcR1 protein (His tag) (AB276266)
  • FuncS

Supplier Data

Functional Studies - Recombinant human DcR1 protein (His tag) (AB276266)

Measured by its binding ability in a functional ELISA. Immobilized human TNFRSF10C at 10 μg/mL (100 μL/well) can bind biotinylated human TNFSF10, the EC50 of biotinylated human TNFSF10 is 0.1-0.7 μg/mL.

SDS-PAGE - Recombinant human DcR1 protein (His tag) (AB276266)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human DcR1 protein (His tag) (AB276266)

SDS-PAGE analysis of ab276266

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Measured by its binding ability in a functional ELISA. Immobilized human TNFRSF10C at 10 μg/mL (100 μL/well) can bind biotinylated human TNFSF10, the EC50 of biotinylated human TNFSF10 is 0.1-0.7 μg/mL.

Accession

O14798

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: PBS

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MARIPKTLKFVVVIVAVLLPVLAYSATTARQEEVPQQTVAPQQQRHSFKGEECPAGSHRSEHTGACNPCTEGVDYTNASNNEPSCFPCTVCKSDQKHKSSCTMTRDTVCQCKEGTFRNENSPEMCRKCSRCPSGEVQVSNCTSWDDIQCVEEFGANATVETPAAEETMNTSPGTPAPAAEETMNTSPGTPAPAAEETMTTSPGTPAPAAEETMTTSPGTPAPAAEETMITSPGTP","proteinLength":"Fragment","predictedMolecularWeight":"23.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":235,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"O14798","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True
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Specifications

Form

Lyophilized

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General info

Function

Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.

Post-translational modifications

N-glycosylated and O-glycosylated.

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Product protocols

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Target data

Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand.
See full target information TNFRSF10C
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

EMBO reports 23:e54133 PubMed35758160

2022

Engagement of TRAIL triggers degranulation and IFNγ production in human natural killer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Johannes Höfle,Timo Trenkner,Nadja Kleist,Vera Schwane,Sarah Vollmers,Bryan Barcelona,Annika Niehrs,Pia Fittje,Van Hung Huynh-Tran,Jürgen Sauter,Alexander H Schmidt,Sven Peine,Angelique Hoelzemer,Laura Richert,Marcus Altfeld,Christian Körner
View all publications
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