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Biotinylated Human CTLA-4/CD152 Protein 4752



  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Lys36-Asp161
SKU: 4752parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
product tag

C-His-Avi, also biotinylated

Biotinylated Human CTLA-4/CD152 Protein 4752

Size and concentration
100, 500µg and lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
> 95% as determined by Tris-Bis PAGE
target relevance
CTLA-4 (cytotoxic T-lymphocyte-associated protein 4), also known as CD152, is a protein receptor that, functioning as an immune checkpoint, downregulates immune responses.CTLA4 is constitutively expressed in regulatory T cells but only upregulated in conventional T cells after activation – a phenomenon which is particularly notable in cancers. It acts as an "off" switch when bound to CD80 or CD86 on the surface of antigen-presenting cells.
Protein names
Cytotoxic T-lymphocyte protein 4 (Cytotoxic T-lymphocyte-associated antigen 4) (CTLA-4) (CD antigen CD152)
Gene names
FUNCTION: Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28. {ECO:0000269|PubMed:16551244, ECO:0000269|PubMed:1714933}.
Subellular location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18468488, ECO:0000269|PubMed:28484017}; Single-pass type I membrane protein {ECO:0000269|PubMed:18468488, ECO:0000269|PubMed:28484017}. Note=Exists primarily an intracellular antigen whose surface expression is tightly regulated by restricted trafficking to the cell surface and rapid internalization.
TISSUE SPECIFICITY: Widely expressed with highest levels in lymphoid tissues. Detected in activated T-cells where expression levels are 30- to 50-fold less than CD28, the stimulatory coreceptor, on the cell surface following activation. {ECO:0000269|PubMed:10493833, ECO:0000269|PubMed:16551244, ECO:0000269|PubMed:1713603}.
SUBUNIT: Homodimer; disulfide-linked (PubMed:11279501, PubMed:11279502, PubMed:21156796, PubMed:28484017, Ref.23). Binds to CD80/B7-1 and CD86/B7.2 (PubMed:11279501, PubMed:11279502, PubMed:28484017). Interacts with ICOSLG (PubMed:28484017). {ECO:0000269|PubMed:11279501, ECO:0000269|PubMed:11279502, ECO:0000269|PubMed:21156796, ECO:0000269|PubMed:28484017, ECO:0000269|Ref.23}.
Post-translational modification
PTM: N-glycosylation is important for dimerization. {ECO:0000269|PubMed:11279502, ECO:0000269|PubMed:16002699, ECO:0000269|PubMed:21156796}.; PTM: Phosphorylation at Tyr-201 prevents binding to the AP-2 adapter complex, blocks endocytosis, and leads to retention of CTLA4 on the cell surface. {ECO:0000269|PubMed:10842319, ECO:0000269|PubMed:9175836, ECO:0000269|PubMed:9813138}.
Target Relevance information above includes information from UniProt accession : P16410
The UniProt Consortium


ELISA with Biotinylated Human CTLA-4/CD152 Protein
Immobilized Biotinylated Human CTLA-4, His Tag at 1µg/ml (100µl/Well) on the streptavidin precoated plate (5µg/ml). Dose response curve for Human B7-1, hFc Tag with the EC50 of 2.4ng/ml determined by ELISA (QC Test).
ELISA with Biotinylated Human CTLA-4/CD152 Protein
Immobilized Anti-CTLA-4 Antibody, hFc Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Biotinylated Human CTLA-4, His Tag with the EC50 of 45.7ng/ml determined by ELISA.
HPLC of Biotinylated Human CTLA-4/CD152 Protein
The purity of Biotinylated Human CTLA-4 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Biotinylated Human CTLA-4/CD152 Protein
Biotinylated Human CTLA-4 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



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