Recombinant human CTLA4 protein (Active) is a Human Fragment protein, in the 37 to 162 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, ELISA, FuncS.
A M H V A Q P A V V L A S S R G I A S F V C E Y A S P G K A T E V R V T V L R Q A D S Q V T E V C A A T Y M M G N E L T F L D D S I C T G T S S G N Q V N L T I Q G L R A M D T G L Y I C K V E L M Y P P P Y Y L G I G N G T Q I Y V I D P E P C P D S D F
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application ELISA | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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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.
CD152, CTLA4, Cytotoxic T-lymphocyte protein 4, Cytotoxic T-lymphocyte-associated antigen 4, CTLA-4
Recombinant human CTLA4 protein (Active) is a Human Fragment protein, in the 37 to 162 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, ELISA, FuncS.
Measured by its binding ability in a functional ELISA. Immobilized Human B7-2, Fc Tag (ab167720) at 2μg/mL (100 μL/well) can bind ab167727 with a linear range of 1-6.4 ng/mL.
Measured by its binding ability in an SPR assay. Yervoy (Ipilimumab, Human IgG1) captured on CM5 chip via anti-human IgG Fc antibodies surface, can bind ab167727 with an affinity constant of 25.7 nM.
pH: 7.4
Constituents: 99% PBS
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.
N-glycosylation is important for dimerization.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
CTLA-4 also known as CD152 is an immune checkpoint receptor with a molecular weight of approximately 34 kDa. This protein is expressed on the surface of T-cells especially after activation and sometimes on regulatory T-cells (Tregs). CTLA-4 competes with CD28 for binding to the same ligands CD80 and CD86 on antigen-presenting cells. Unlike CD28 which stimulates T-cell activation CTLA-4 sends inhibitory signals to downregulate immune responses. By doing this CTLA-4 helps maintain immune system homeostasis and prevents autoimmune reactions.
The CTLA-4 protein functions as a critical regulator of the immune system. It interacts with CD80/CD86 in a complex that effectively transmits inhibitory signals to T-cells. CTLA-4 controls the amplitude of the initial activation of T-cells ensuring that the body's immune responses are kept under control. In regulatory T-cells CTLA-4 engagement contributes to their immunosuppressive functions through which they maintain tolerance to self-antigens and prevent overactive immune reactions.
CTLA-4 involves itself in the adaptive immune response pathways specifically the regulation of T-cell activity. CTLA-4's interaction with CD80/CD86 modulates pathways associated with TCR (T-cell receptor) signaling. When CTLA-4 binds its ligands it recruits phosphatases such as SHP-2 that dephosphorylate signaling proteins leading to the downregulation of T-cell interaction. This pathway interaction exemplifies how CTLA-4 acts in concert with proteins like CD28 to finely tune immune responses.
CTLA-4 plays a role in autoimmune diseases and cancer. The dysregulation of CTLA-4 function can lead to autoimmune disorders where the immune system attacks the body's own tissue. In cancer tumor cells may manipulate CTLA-4 pathways to evade immune surveillance. Targeted therapies like anti-CTLA-4 antibodies such as ipilimumab have been developed to block CTLA-4 aiming to enhance the immune system’s ability to attack cancer cells. These treatments highlight the role of CTLA-4 in balancing immune activity and the potential to alter this balance for therapeutic benefit.
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SDS-PAGE of reduced ab167727 stained overnight with Coomassie Blue. The protein migrates as 25-30 kDa under reducing conditions due to glycosylation.
Immobilized Human B7-1, Fc Tag (Recombinant human CD80 protein (Active) ab173993) at 2μg/mL (100 μL/well) can bind ab167727 with a linear range of 0.16-2.56 ng/mL.
Immobilized Human B7-2, Fc Tag (Recombinant human CD86 protein (Fc Chimera) ab167720) at 2μg/mL (100 μL/well) can bind ab167727 with a linear range of 1-6.4 ng/mL.
Yervoy (Ipilimumab, Human IgG1) captured on CM5 chip via anti-human IgG Fc antibodies surface, can bind ab167727 with an affinity constant of 25.7 nM as determined in SPR assay.
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