webinar
Oct. 27-28, 2025, Boston, MA, USA - Booth 114.
Read More

N-Succinimidyl 4-(N-maleimidomethyl) trans-cyclohexane 1-carboxylate

  CAS No.: 71875-81-5   Cat No.: BADC-00503   Purity: ≥98% 4.5  

N-Succinimidyl 4-(N-maleimidomethyl) trans-cyclohexane 1-carboxylate is an essential compound in the biomedical sector that exhibits high complexity and variability in its applications. Acting as a reactive linker, it facilitates the conjugation of biomolecules to proteins, peptides, or drugs, thereby enabling targeted therapeutic delivery for addressing diverse ailments including cancer and autoimmune disorders. Embracing this compound empowers the biomedical industry to explore innovative means of combating diseases.

N-Succinimidyl 4-(N-maleimidomethyl) trans-cyclohexane 1-carboxylate

Structure of 71875-81-5

Quality
Assurance

Worldwide
Delivery

24/7 Customer
Support
Category
ADC Linker
Molecular Formula
C16H18N2O6
Molecular Weight
334.32
Shipping
Room temperature
Shipping
Store at -20°C

* For research and manufacturing use only. We do not sell to patients.

Size Price Stock Quantity
-- $-- In stock

Looking for different specifications? Click to request a custom quote!

Capabilities & Facilities

Popular Publications Citing BOC Sciences Products
Synonyms
Cyclohexanecarboxylic acid, 4-[(2,5-dihydro-2,5-dioxo-1H-pyrrol-1-yl)methyl]-, 2,5-dioxo-1-pyrrolidinyl ester, trans-; 1H-Pyrrole-2,5-dione, 1-[[4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]cyclohexyl]methyl]-, trans-; 1H-Pyrrole-2,5-dione, 1-[[trans-4-[[(2,5-dioxo-1-pyrrolidinyl)oxy]carbonyl]cyclohexyl]methyl]-; 2,5-Dioxo-1-pyrrolidinyl trans-4-[(2,5-dihydro-2,5-dioxo-1H-pyrrol-1-yl)methyl]cyclohexanecarboxylate; trans-4-Maleimidylmethylcyclohexylcarboxylic acid 2,5-dioxopyrrolidin-1-yl ester
IUPAC Name
2,5-dioxopyrrolidin-1-yl (1r,4r)-4-((2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)methyl)cyclohexane-1-carboxylate
Canonical SMILES
O=C1C=CC(=O)N1CC2CCC(C(=O)ON3C(=O)CCC3=O)CC2
InChI
InChI=1S/C16H18N2O6/c19-12-5-6-13(20)17(12)9-10-1-3-11(4-2-10)16(23)24-18-14(21)7-8-15(18)22/h5-6,10-11H,1-4,7-9H2/t10-,11-
InChIKey
JJAHTWIKCUJRDK-XYPYZODXNA-N
Density
1.42±0.1 g/cm3
Solubility
Soluble in Acetone, Methanol
Melting Point
171-174°C
Appearance
Soild powder
Shipping
Room temperature
Storage
Store at -20°C
Pictograms
Irritant
Signal Word
Warning
Boiling Point
501.7±42.0°C at 760 mmHg
In Vitro
The in vitro cytotoxic activities of CX and SMCC ADCs were similar for several cancer cell lines; however, the CX ADC was more active (5-100-fold lower IC50) than the SMCC ADC in other cell lines, including a multidrug-resistant line.
In Vivo
Both CX and SMCC ADCs showed comparable MTDs and pharmacokinetics in CD-1 mice. In Calu-3 tumor xenografts, antitumor efficacy was observed with the anti-EpCAM CX ADC at a 5-fold lower dose than the corresponding SMCC ADC in vivo Similarly, the anti-EGFR CX ADC showed improved antitumor activity over the respective SMCC conjugate in HSC-2 and H1975 tumor models; however, both exhibited similar activity against FaDu xenografts. Mechanistically, in contrast with the charged lysine-linked catabolite of SMCC ADC, a significant fraction of the carboxylic acid catabolite of CX ADC could be uncharged in the acidic lysosomes, and thus diffuse out readily into the cytosol. Upon release from tumor cells, CX catabolites are charged at extracellular pH and do not penetrate and kill neighboring cells, similar to the SMCC catabolite.
1. Targeting HER2-positive breast cancer with trastuzumab-DM1, an antibody-cytotoxic drug conjugate
Ralph H Schwall, Elaine Mai, Ravi V J Chari, Susan D Spencer, Walter A Blättler, Debra L Dugger, Sara R Kenkare-Mitra, John M Lambert, Gail D Lewis Phillips, Lisa M Crocker, Mark X Sliwkowski, Guangmin Li, Robert J Lutz, Hartmut Koeppen, Kathryn L Parsons, Wai Lee T Wong, Frederic S Jacobson Cancer Res . 2008 Nov 15;68(22):9280-90. doi: 10.1158/0008-5472.CAN-08-1776.
HER2 is a validated target in breast cancer therapy. Two drugs are currently approved for HER2-positive breast cancer: trastuzumab (Herceptin), introduced in 1998, and lapatinib (Tykerb), in 2007. Despite these advances, some patients progress through therapy and succumb to their disease. A variation on antibody-targeted therapy is utilization of antibodies to deliver cytotoxic agents specifically to antigen-expressing tumors. We determined in vitro and in vivo efficacy, pharmacokinetics, and toxicity of trastuzumab-maytansinoid (microtubule-depolymerizing agents) conjugates using disulfide and thioether linkers. Antiproliferative effects of trastuzumab-maytansinoid conjugates were evaluated on cultured normal and tumor cells. In vivo activity was determined in mouse breast cancer models, and toxicity was assessed in rats as measured by body weight loss. Surprisingly, trastuzumab linked to DM1 through a nonreducible thioether linkage (SMCC), displayed superior activity compared with unconjugated trastuzumab or trastuzumab linked to other maytansinoids through disulfide linkers. Serum concentrations of trastuzumab-MCC-DM1 remained elevated compared with other conjugates, and toxicity in rats was negligible compared with free DM1 or trastuzumab linked to DM1 through a reducible linker. Potent activity was observed on all HER2-overexpressing tumor cells, whereas nontransformed cells and tumor cell lines with normal HER2 expression were unaffected. In addition, trastuzumab-DM1 was active on HER2-overexpressing, trastuzumab-refractory tumors. In summary, trastuzumab-DM1 shows greater activity compared with nonconjugated trastuzumab while maintaining selectivity for HER2-overexpressing tumor cells. Because trastuzumab linked to DM1 through a nonreducible linker offers improved efficacy and pharmacokinetics and reduced toxicity over the reducible disulfide linkers evaluated, trastuzumab-MCC-DM1 was selected for clinical development.
2. Effect of trypsin concentration on living SMCC-7721 cells studied by atomic force microscopy
Li Li, Jin Yan, Zuobin Wang, Chenchen Xie, Zhengxun Song, Jiajing Zhu J Microsc . 2021 Dec;284(3):203-213. doi: 10.1111/jmi.13053.
Trypsin is playing an important role in the processes of cancer proliferation, invasion and metastasis which require the precise information of morphology and mechanical properties on the nano-scale for the related research. In this work, living human hepatoma (SMCC-7721) cells were treated with different concentrations of trypsin solution. The morphology and mechanical properties of the cells were measured via atomic force microscope (AFM). Statistical analyses of measurement data indicated that with the increase of trypsin concentration, the average cell height and the surface roughness were both increased, but the cell viability, the cell surface adhesion and the elasticity modulus were decreased significantly. The force required to puncture the cells was also gradually reduced. It indicates that trypsin not only hydrolyses the proteins between the cell and the substrate but also the membrane proteins. The results offer valuable clues for the cancerous process study, pathological analysis and trypsin inhibitor drug development. And this work provides an effective way for overcoming the cell membrane in drug injection for cell-targeted therapy.
3. TRAP/SMCC/mediator-dependent transcriptional activation from DNA and chromatin templates by orphan nuclear receptor hepatocyte nuclear factor 4
Sohail Malik, Robert G Roeder, Yun Kyoung Kang, Annika E Wallberg Mol Cell Biol . 2002 Aug;22(15):5626-37. doi: 10.1128/MCB.22.15.5626-5637.2002.
The orphan nuclear receptor hepatocyte nuclear factor 4 (HNF-4) regulates the expression of many liver-specific genes both during development and in the adult animal. Towards understanding the molecular mechanisms by which HNF-4 functions, we have established in vitro transcription systems that faithfully recapitulate HNF-4 activity. Here we have focused on the coactivator requirements for HNF-4, especially for the multicomponent TRAP/SMCC/Mediator complex that has emerged as the central regulatory module of the transcription apparatus. Using a system that has been reconstituted from purified transcription factors, as well as one consisting of unfractionated nuclear extract from which TRAP/SMCC/Mediator has been depleted by specific antibodies, we demonstrate a strong dependence of HNF-4 function on this coactivator. Importantly, we further show a TRAP/SMCC/Mediator-dependence for HNF-4 transcriptional activation from chromatin templates. The latter involves cooperation with the histone acetyltransferase-containing coactivator p300, in accord with a synergistic mode of action of the two divergent coactivators. We also show that HNF-4 and TRAP/SMCC/Mediator can interact physically. This interaction likely involves primary HNF-4 activation function 2 (AF-2)-dependent interactions with the TRAP220 subunit of TRAP/SMCC/Mediator and secondary (AF-2-independent) interactions with TRAP170/RGR1. Finally, recruitment experiments using immobilized templates strongly suggest that the functional consequences of the physical interaction probably are manifested at a postrecruitment step in the activation pathway.

The molarity calculator equation

Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Related Products

Contact our experts today for pricing and comprehensive details on our ADC offerings.

You May Also Be Interested In

From cytotoxin synthesis to linker design, discover our specialized services that complement your ADC projects.

ADC Linker Development Enzyme Cleavable Linker Cathepsin B Cleavable Linker/Peptide Linker Phosphatase Cleavable Linker β-Glucuronide Linker β-Galactosidase Cleavable Linker Sulfatase Cleavable Linker Chemically Cleavable Linker Non-Cleavable Linker Services Acid Cleavable Linker/Hydrazone Linker

Unlock Deeper ADC Insights

Learn more about payload design, linker strategies, and integrated CDMO support through our curated ADC content.

Linkers - A Crucial Factor in Antibody–Drug Conjugates In-Depth Review of ADC Linkers: Types, Mechanisms, and Research Progress New Structural Insights Solve Instability Issues of Maleimide Linkers in ADCs PEG Linkers in Antibody-Drug Conjugates Peptide Linkers in Antibody-Drug Conjugates Disulfide Linkers in Antibody-Drug Conjugates Biotinylation Reagents in Antibody-Drug Conjugates Maleimide Linkers in Antibody-Drug Conjugates Current ADC Linker Chemistry SPDB Linkers in Antibody-Drug Conjugates

Explore More ADC Products

Find exactly what your project needs from our expanded range of ADCs, offering flexible options to fit your timelines and goals.

ADC Cytotoxin

Powerful Targeted Cancer Solutions

ADC  Cytotoxin with Linker

Enhanced Stability And Efficacy

ADC Linker

Precise Conjugation For Success

Antibody-Drug  Conjugates (ADCs)

Maximized Therapeutic Performance

Auristatins

Next-Level Tubulin Inhibition

Calicheamicins

High-Impact DNA Targeting

Camptothecins

Advanced Topoisomerase Inhibition

Daunorubicins / Doxorubicins

Trusted Anthracycline Payloads

Duocarmycins

Potent DNA Alkylation Agents

Maytansinoids

Superior Microtubule Disruption

Pyrrolobenzodiazepines

Ultra-Potent DNA Crosslinkers

Traditional Cytotoxic Agents

Proven Chemotherapy Solutions

Cleavable Linker

Precise Intracellular Drug Release

Non-Cleavable Linker

Exceptional Long-Term Stability

Historical Records: SPDP-C6-Gly-Leu-NHS ester | Tusamitamab ravtansine | Val-Cit-PAB-MMAF | SPDPH | Sirtratumab vedotin | Patritumab deruxtecan | Fmoc-D-Val-Cit-PAB | N-succinimidyl 4-(5-nitro-pyridin-2-yldithio)-pentanoate | Cantuzumab mertansine | Disitamab vedotin | N-Succinimidyl 4-(N-maleimidomethyl) trans-cyclohexane 1-carboxylate
Send Inquiry
Verification code
Inquiry Basket