N-Succinimidyl 4-(maleimidomethyl)cyclohexanecarboxylate NEW

N-Succinimidyl 4-(maleimidomethyl)cyclohexanecarboxylate (SMCC) is a heterobifunctional crosslinking reagent commonly used to conjugate biomolecules. Its key features are:

Two Reactive Groups:

• N-Hydroxysuccinimide (NHS) Ester: Reacts specifically with primary amines (-NH₂, e.g., on lysine residues or protein N-termini) to form stable amide bonds.

• Maleimide Group: Reacts specifically with sulfhydryl groups (-SH, e.g., on cysteine residues) via thioether bonds.

  Spacer: The cyclohexane ring provides a rigid, hydrophobic spacer (~11.6 Å) separating the two reactive ends. This structure enhances the stability of the maleimide group against hydrolysis compared to similar linkers with linear alkyl spacers.

  Primary Function: To covalently link an amine-containing molecule (e.g., an antibody, protein, or amine-modified nucleic acid) to a thiol-containing molecule (e.g., a peptide, toxin, drug, enzyme, or thiol-modified oligonucleotide). The reaction is typically performed sequentially: NHS-ester first with the amine, then maleimide with the thiol.

  Key Applications:

• Antibody-Drug Conjugates (ADCs): Linking cytotoxic drugs to antibodies.

• Enzyme-Antibody Conjugates: Creating immunoenzymes for ELISA/diagnostics.

• Protein-Protein/Protein-Peptide Conjugates.

• Immobilization: Attaching proteins/peptides to surfaces or carriers functionalized with amines or thiols.

• Bioconjugation research.

  Handling: Typically supplied as a solid. Soluble in anhydrous DMSO or DMF. Moisture-sensitive; store desiccated at ≤ -20°C.

In short: SMCC is a versatile, stable crosslinker designed for specific, stepwise conjugation of amine- and thiol-containing molecules, widely used in bioconjugation, especially for ADCs and diagnostics.