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| Description | Adds a Cys-Gly-Lys-Arg spacer to the Aβ42 N-terminus; the free thiol enables site-specific maleimide coupling to carriers, beads or solid supports for immunogens and affinity ligands. |
Product Basic Information Table
| Standard English Name | Abbreviations/Aliases | Functional Tags | Structural Core | Molecular Formula | Exact MW (Da) | Average MW (Da) | Salt Form | Length (aa) |
| Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42) | CGKR-Aβ(1-42); N-terminal Cys-conjugatable Aβ42; Cys-Gly-Lys-Arg spacer Aβ42; thiol-site-directed labeling Aβ42 | N-terminal free Cys thiol, CGKR tetrapeptide spacer, thiol site-directed conjugation (maleimide/iodoacetamide), immobilization/crosslinking, requires anti-oxidation/anti-dimerization, strong aggregation / mandatory HFIP | Linear 46-mer, sequence CGKRDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA (an N-terminal Cys-Gly-Lys-Arg tetrapeptide spacer linked by a peptide bond to the N terminus of native Aβ1-42, i.e. CGKR-Aβ42). The N terminus carries a free cysteine thiol (–SH), followed by the Gly-Lys-Arg spacer, then the native Aβ(1-42) body; the Aβ portion has a free N-terminal amine and free C-terminal carboxylate (non-amidated) and contains Met35. The free thiol reacts efficiently and site-specifically with maleimide, iodoacetamide and disulfide-activated resins, enabling fluorescent/biotin labeling, solid-support/magnetic-bead immobilization and crosslinking; the CGKR spacer also adds N-terminal hydrophilicity and reduces steric hindrance. The free thiol is prone to oxidation into Cys-Cys dimers-store under inert gas and add reductant when needed. | C220H343N63O64S2 | 4955.50 | 4958.66 | TFA salt (with free Cys thiol); CAS 1802086-21-0 | 46 |
Physicochemical Solubility & Storage Parameters
| Product Code | Appearance | Long-term Storage | Short-term Storage | Solution Stability | Solid Stability |
| PEP-ABCGKR-01 | White to off-white powder | Store at −20°C, sealed, desiccated, protected from light; because of the free thiol, vacuum-seal then flush with argon/nitrogen and aliquot to avoid freeze-thaw and oxidative dimerization; ~2 years; add reductant per protocol for long-term storage if required. | Brief shipping/storage at 2–8°C (~1 week), sealed under inert gas; handle working solutions on ice under low-oxidation conditions, add TCEP/DTT fresh as needed and use immediately; aliquot for −80°C; ship on dry ice or ample blue ice. | The Aβ42 body aggregates strongly, so **HFIP de-aggregation is mandatory**: dissolve the lyophilate in HFIP (~1–2 mM), sonicate on ice 5–10 min, aliquot and evaporate to a monomeric film under vacuum, store at −20°C under inert gas; before use, dissolve in dilute NaOH (~pH 10) then neutralize into pH 7.4 PBS and use fresh on ice. **Thiol protection**: the aqueous –SH readily oxidizes into disulfide dimers; thaw fresh and add 10–50 μmol/L TCEP (or DTT) before conjugation, then perform maleimide/iodoacetamide coupling quickly (<1 h); thoroughly remove free reductant afterward to avoid competition. Do not keep solutions at 4°C beyond a few days-aliquot and store at −80°C under inert gas; never leave at room temperature; avoid repeated freeze-thaw. | solid stable ~2 years at −20°C, sealed, desiccated, light-protected, under argon/nitrogen; hygroscopic and oxidation-prone-keep dry/dark/sealed and under inert gas; minimize repeated opening; contains Met35. |
Functional Description
| Product Code | Short Summary (listing) | Detailed Biological Function | Research Areas | Targets/Receptors |
| PEP-ABCGKR-01 | A 46-mer conjugatable tool peptide in which native Aβ(1-42) is extended at its N terminus by a Cys-Gly-Lys-Arg (CGKR) tetrapeptide spacer. The N-terminal free cysteine thiol reacts site-specifically with maleimide/iodoacetamide for fluorescent/biotin labeling, magnetic-bead/resin immobilization, pull-down and crosslinking; the CGKR arm adds hydrophilic flexibility and reduces steric hindrance. Free thiol requires anti-oxidation/anti-dimerization; HFIP de-aggregation mandatory; store under inert gas. | Aβ42 is the central target peptide in Alzheimer's research, but full-length Aβ42 is highly hydrophobic and aggregates extremely rapidly; introducing labels directly onto its sequence (e.g. via lysine side chains) often alters charge and aggregation behavior. Fusing a short cysteine-containing tag to the N terminus-here Cys-Gly-Lys-Arg (CGKR) followed by native Aβ(1-42), 46 residues in total-provides a unique, chemically orthogonal handle (a free cysteine thiol, –SH) without modifying the Aβ body. The thiol reacts rapidly and near-quantitatively with maleimide at pH 6.5–7.0 to form a stable thioether (far faster than amine coupling), and also allows alkylation with iodoacetamide or disulfide ligation via pyridyl-disulfide/DTT-activated resins. Typical uses: (1) fluorescent/biotin maleimide labeling to generate monomer-controlled Aβ42 probes for imaging, FRET or aggregation tracking; (2) thiol-directed immobilization onto thiol-activated magnetic beads/resins for pull-down of Aβ42-binding proteins, receptor/chaperone screening and solid-phase aggregation assays; (3) bifunctional-crosslinker-mediated Aβ–receptor or Aβ–membrane-component crosslinking; (4) oriented immobilization on biosensor surfaces for interaction measurements (SPR/BLI). Within the CGKR spacer, Gly provides flexibility and Lys/Arg add local positive charge and aqueous solubility, keeping the tag away from the hydrophobic Aβ core and minimizing interference with conjugation efficiency and aggregation. Cautions: the Aβ42 body aggregates extremely rapidly-always monomerize with HFIP before labeling/immobilization; the free –SH readily oxidizes to intermolecular disulfide dimers in aqueous solution-work under inert/low-oxygen conditions, reduce fresh with TCEP/DTT immediately before coupling, and remove free reductant completely before conjugation; Met35 also requires oxidation protection. | Aβ42 thiol site-directed conjugation, maleimide/iodoacetamide labeling, fluorescent/biotin probe preparation, magnetic-bead/resin immobilization and pull-down, Aβ-binding-protein/receptor screening, crosslinking and solid-phase aggregation, oriented SPR/BLI surface immobilization, free-Cys anti-oxidation/anti-dimerization | Covalently conjugates via the free Cys thiol to maleimide/iodoacetamide probes and thiol-activated solid supports; the Aβ body still self-aggregates into beta-sheet fibrils; no new receptor target-used as a site-directedly conjugatable Aβ42 tool peptide |
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