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Anti-ER-a36 (clone SNGmBI)-SMCC-DM1 ADC (CAT#: ADC-W-205)

This ADC product is comprised of an anti-ER-a36 monoclonal antibody (clone SNGmB) conjugated via a SMCC linker to DM1. The DM1 is targeted to certain cancers by immunerecognition and delivered into cancer cells via receptor mediated endocytosis. Within the cell, DM1 binds to tubulins, interrupts microtubule dynamics, and subsequently, induces cell death.

  • Product Information
  • ADC Target
  • ADC Antibody
  • ADC Linker
  • ADC payload drug
  • Antibody clone #
  • SNGmBI
  • Name
  • ER-a36
  • Alternative Names
  • ER; ESR; Era; ESRA; ESTRR; NR3A1
  • Target Entrez Gene ID
  • 2099
  • Overview
  • This gene is a 36 kDa variant of hER-a, it lacks the N-terminal AF-1 domain and the C-terminal AF-2 domain of hER-a. hER-a is one of the two types of estrogen receptors discovered in human cells (hERs). hERs encodes an estrogen receptor, a ligand-activated transcription factor composed of several domains important for hormone binding, DNA binding, and activation of transcription.
  • Overview
  • Anti-ER-a36 mlgG2b antibody, clone # SNGmBI
  • Clone #
  • SNGmBI
  • Host animal
  • Mouse
  • Species Reactivity
  • Human
  • Name
  • SMCC (N-succinimidyl 4-(Nmaleimidomethyl)cyclohexane-1-carboxylate)
  • Description
  • Noncleavable linkers, is considered noncleavable-meaning linker cleavage, and payload release does not depend on the differential properties between the plasma and some cytoplasmic compartments. Instead, the release of the cytotoxic drug is postulated to occur after internalization of the ADC via antigen-mediated endocytosis and delivery to lysosomal compartment, where the antibody is degraded to the level of amino acids through intracellular proteolytic degradation.
  • Name
  • DM1 (N2’-Deacetyl-N2’-(3-mercapto-1-oxopropyl)maytansine)
  • Description
  • Derived from Maytansinoid,a group of cytotoxins structurally similar to rifamycin, geldanamycin, and ansatrienin. The eponymous natural cytotoxic agent maytansine is a 19-member lactam (ansa
    macrolide) structure originally isolated from the Ethiopian shrub Maytenus ovatus. Maytansinoids can bind to tubulin at or near the vinblastine-binding site, which interfere the formation of microtubules and depolymerize already formed microtubules, inducing mitotic arrest in the intoxicated cells.

For Research Use Only. NOT FOR CLINICAL USE.

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