Key features and details
- Purity: > 90% n/a
- Suitable for: Blocking
Product nameHuman S1P peptide
Purity> 90 % n/a.
Our Abpromise guarantee covers the use of ab223083 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Blocking - Blocking peptide for Anti-S1P antibody (ab140592)
Blocking peptide for 140592
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C.
Information available upon request.
- kexin isozyme 1
RelevanceS1P (also known as MBTPS1,SKI1), was first discovered as one of two enzymes that cleave the sterol regulatory binding proteins (SREBPs), in the case of S1P at “site-1,” a hydrophillic loop extending into the lumen of the ER. The MBTPS1 domain structure contains a signal sequence followed by a propeptide domain, a catalytic domain, a transmembrane domain and a cytoplasmic domain.
Cellular localizationEndoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein.
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab223083 has not yet been referenced specifically in any publications.