Anti-DR5 (Apomab) h(CD28-CD3ζ) CAR, pSBCAR1 vector

All products and services are For Research Use Only and CANNOT be used in the treatment or diagnosis of disease.

Details

Target
DR5

Targeting Cell Type
T cell

Targeting Diseases
Lung malignancy

Generation
Second

Vector Name
pSBCAR1

Vector Length
~6kb

Vector Type
Sleeping Beauty (SB) transposon

Receptor Construction
scFv-CD28-CD3ζ

Discription of Signaling Cassetes
CD28
CD28 (Cluster of Differentiation 28) is one of the proteins expressed on T cells that provide costimulatory signals required for T cell activation and survival. CD28 is the receptor for CD80 (B7.1) and CD86 (B7.2) proteins which are expressed on antigen-presenting cells (APC). CD28 modulates the primary TCR/CD3ζ signal in a different fashion than the late costimulatory elements OX40 and 4-1BB. CD28 enhances the expression of downstream regulators that impact on T-cell proliferation, death, differentiation, and effector functions. CAR+ T cells containing the CD28 endodomain showed strikingly enhanced sustained T cell activation, growth, survival. And CD28 results in a brightly expressed, stable receptor as the transmembrane domain. Including CD28 costimulatory domains in CARs led to enhanced anti-malignancy efficacy.
CD3ζ
CD3ζ, also known as T-cell receptor zeta, which together with T-cell receptor and CD3γ, δ, ε chain, forms the TCR-CD3 complex. ζ was expressed independently from the complex. The zeta chain plays an important role in coupling antigen recognition to several intracellular signal-transduction pathways. CD3-zeta, which contains 3 ITAMs, is the most commonly used endodomain component of CARs. It transmits an activation signal to the T cell after antigen is bound. CD3-zeta may not provide a fully competent activation signal and additional co-stimulatory signaling is needed. For example, chimeric CD28 and OX40 can be used with CD3-zeta to transmit a proliferative/survival signal, or all three can be used together.

Target

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Published Data

CAR scFv data FCM

Fig.2 The percentage of total surface DR5 was analyzed at the indicated times using a combination of commercial and indicated DR5 antibodies with or without crosslinking with PFA.

CAR Construction :

Fig.2 The percentage of total surface DR5 was analyzed at the indicated times using a combination of commercial and indicated DR5 antibodies with or without crosslinking with PFA.

All measurements were performed in triplicate.

Shivange, G., Mondal, T., Lyerly, E., Bhatnagar, S., Landen, C. N., Reddy, S., ... & Tushir-Singh, J. (2021). A patch of positively charged residues regulates the efficacy of clinical DR5 antibodies in solid tumors. Cell reports, 37(5), 109953.

CAR scFv data FCM

Fig.3 The percentage of total surface DR5 was analyzed using flow cytometry at the indicated times using a combination of commercial and indicated DR5 agonist antibodies.

CAR Construction :

Fig.3 The percentage of total surface DR5 was analyzed using flow cytometry at the indicated times using a combination of commercial and indicated DR5 agonist antibodies.

Data are representative of triplicates.

CAR scFv data FCM

Fig.4 The apoptosis inducing activity of TR2-3 detected in cancer cells and normal cells.

CAR Construction :

Fig.4 The apoptosis inducing activity of TR2-3 detected in cancer cells and normal cells.

These data are representative of at least three independent experiments.

Lei, G., Xu, M., Xu, Z., Gu, L., Lu, C., Bai, Z., ... & Tan, S. (2017). A novel fully human agonistic single chain fragment variable antibody targeting death receptor 5 with potent antitumor activity in vitro and in vivo. International journal of molecular sciences, 18(10), 2064.

CAR scFv data ELISA

Fig.1 Saturation analysis. Apomab was labeled with 125I and incubated at the indicated concentrations with DR5-Fc-coated on microtiter wells for 1 h at room temperature. Nonspecific binding was determined in the presence of excess unlabeled Apomab.

CAR Construction :

A nonlinear one-site curve fit indicated a KD of 0.92±0.01 nM

Adams, C., Totpal, K., Lawrence, D., Marsters, S., Pitti, R., Yee, S., ... & Ashkenazi, A. (2008). Structural and functional analysis of the interaction between the agonistic monoclonal antibody Apomab and the proapoptotic receptor DR5. Cell Death & Differentiation, 15(4), 751-761.

More Published Data More Published Data

For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

Anti-DR5 (Apomab) h(CD28-CD3ζ) CAR, pSBCAR1 (CAR-SB-LX0200)

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