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[Val35]-Amyloid β-Protein (1–42), also described as M35V Aβ42, is an engineered analog of human Aβ42 in which the native methionine at position 35 is replaced by valine.
The substitution removes the sulfur-containing methionine side chain while retaining a hydrophobic residue at the same position.
Product Information
| Property | Specification |
|---|---|
| Product Name | [Val35]-Amyloid β-Protein (1–42) |
| Mutation | M35V |
| Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLVVGGVVIA |
| Length | 42 amino acids |
| Molecular Formula | C203H311N55O60 |
| Theoretical MW | ~4482.05 Da |
| Parent Peptide | Human Aβ42 |
| Peptide Type | Site-specific Aβ42 analog |
| Research Areas | Met35 chemistry, oxidation, membrane interaction, aggregation |
Why Met35 Is an Important Experimental Variable
Methionine 35 has been studied in relation to oxidative chemistry, peptide–membrane interaction and Aβ-associated cellular effects.
Replacing Met35 with valine allows investigators to test whether a measured response specifically requires the sulfur-containing methionine side chain.
Because valine remains hydrophobic, the substitution provides a more focused comparison than replacing Met35 with a strongly polar residue.
Recommended Comparator
Wild-type human Aβ42 is the most appropriate primary comparator.
We recommend preparing the native and M35V peptides under the same solvent, concentration and incubation conditions because differences in aggregation state can otherwise complicate interpretation of residue-specific effects.
Analytical identity and purity can be documented through Peptide Quality Control.
Frequently Asked Questions
What does [Val35]-Aβ42 mean?
[Val35]-Aβ42 is an Aβ42 analog containing an M35V substitution, meaning the native methionine at residue 35 has been replaced by valine.
Why is Met35 important in Aβ research?
Met35 contains a sulfur-containing side chain that has been investigated in relation to oxidation, membrane interactions, oxidative stress, and Aβ-associated cellular effects. M35V allows researchers to investigate the specific contribution of this methionine residue.
Does M35V remove the hydrophobic character of position 35?
No. Valine remains strongly hydrophobic. The substitution primarily removes the sulfur-containing chemistry of methionine while maintaining a nonpolar side chain at the same position.
What is the best control for [Val35]-Aβ42?
Wild-type human Aβ42 is the most appropriate direct comparator. Both peptides should be handled under matched conditions because differences in aggregation state can otherwise be mistaken for effects caused by the M35V substitution.
Research Use Only.