| Catalog No. | HX200026 |
|---|
| Species reactivity | Human |
|---|
| Applications | ELISA, Bioactivity: FACS, Functional assay, Research in vivo |
|---|
| Host species | Human |
|---|
| Isotype | IgG1-lambda |
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| Clone ID | D8P1C1 |
|---|
| Biological activity |
and tumor growth in xenograft models. 89 Zr-DFO-D8P1C1 radioimmunological PET imaging shows its substantial accumulation in ovarian tumor xenografts, serving as a platform for generating bispecific T-cell engager derivatives. D8P1C1 can be applied to research on related diseases including triple-negative breast cancer, various types of ovarian cancer, lung adenocarcinoma, glioma, and colon cancer [1] [2] [3]. . D8P1C1 (10 ug/mL; 4 h) potently inhibits EGFR phosphorylation in MDA-MB-231, HCC-827, OVCAR-3, and SKOV-3 cells [1]. D8P1C1 (0.037 ug/mL; 38 h) inhibits proliferation of triple-negative breast cancer MDA-MB-231 cells with an IC 50 of 0.037 ug/mL [2]. D8P1C1 (0.625-20 ug/mL; 38 h) inhibits proliferation of SKBR-3, HCC-827, LIM1215, U-87 MG, SKOV-3, OVCAR-3, and CAOV-3 cancer cells, with the greatest efficacy observed in HER2-overexpressing breast SKBR-3 cells [2]. D8P1C1 (7.8125-250 uM; 2 h) preferentially binds to ADAM17 expressed on MDA-MB-231, SKBR-3, HCC-827, LIM1215, U-87 MG, OVCAR-3, SKOV-3, and CAOV-3 cancer cells, with binding affinity approximately 6-fold higher than for ADAM17 on HEK293 cells [2]. . Inhibited TNFα shedding by 78%, CX3CL1 shedding by 70%, and Notch1 cleavage (measured as NICD1 release) by 15%. . Showed no significant change in total EGFR levels in most cell lines. D8P1C1 (40 mg/kg; i.p.; bi-weekly; 4 weeks) achieves 25. |
| Expression system |
Mammalian cells |
| Clonality |
Monoclonal |
| Target |
TACE, Snake venom-like protease, ADAM17, CD156b, CSVP, ADAM 17, Disintegrin and metalloproteinase domain-containing protein 17, TNF-alpha convertase, TNF-alpha-converting enzyme |
| Endotoxin level |
Please contact the lab for this information. |
| Purity |
>95% purity as determined by SDS-PAGE. |
| Purification |
Protein A/G purified from cell culture supernatant. |
| Accession |
P78536 |
| Form |
Liquid |
| Storage buffer |
0.01M PBS pH 7.4 Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
|
| Stability and Storage |
Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Alternate Names | D8P1C1 |
|---|
| Background | Disintegrin and metalloproteinase domain-containing protein 17 (CD156b/ADAM17) is a ~93 kDa protein. Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins including adhesion proteins, growth factor precursors and cytokines important for inflammation and immunity. Cleaves the membrane-bound precursor of TNF to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). 2. Heurich, A. et al. (2014) Journal of virology 88, 1293-307. PMID: 242278433. Riethmueller, S. et al. (2017) PLoS biology 15, e2000080. PMID: 280608204. Feuerbach, D. et al. (2017) Neuroscience letters 660, 109-114. PMID: 289234817. Rabquer, BJ. et al. (2010) Journal of immunology (Baltimore, Md. : 1950) 185, 1777-85. PMID: 205922838. Thathiah, A. et al. (2003) The Journal of biological chemistry 278, 3386-94. PMID: 12441351 |
|---|
| References |
1. Saha N, et al. Characterization of the D8P1C1 Anti-ADAM17 Inhibitory Monoclonal Antibody and Generation of Its Bispecific T-Cell Engager Derivative. Int J Mol Sci. 2026;27(7):2936. Published 2026 Mar 24. [HX200026]
2. Saha N, et al. Inhibitory monoclonal antibody targeting ADAM17 expressed on cancer cells. Transl Oncol. 2022;15(1):101265. [HX200026]
3. Arora S, et al. ADAM Proteases in Cancer: Biological Roles, Therapeutic Challenges, and Emerging Opportunities. Cancers (Basel). 2025;17(10):1703. Published 2025 May 19. [HX200026] |
| Note |
For research use only. Not suitable for clinical or therapeutic use. |
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