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Invitrogen
Human SCAMP2 (aa 1-17) Synthetic Peptide
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Product Details
PEP-151
Product Specifications
Class
Synthetic
Type
Peptide
Conjugate
Unconjugated
Unconjugated
Unconjugated
Form
Lyophilized
Concentration
0.5 mg/mL
Amount
50 µg
Storage conditions
-20°C, Avoid Freeze/Thaw Cycles
Shipping conditions
Wet ice
Product Specific Information
PEP-151 is a 17 amino acid synthetic peptide whose sequence is from human SCAMP 2. The sequence of this peptide is (amino to carboxy terminus): M (1)-S-A-F-D-T-N-P-F-A-D-P-V-D-V-N-P (17)-C
This peptide may be used for neutralization and control experiments with the polyclonal antibody that reacts with this product and human SCAMP 2, catalog # PA1-734. Using a solution with equal weights per unit volume of peptide and corresponding antibody will yield a solution with a large molar excess of peptide that is able to competitively bind the antibody.
Reconstitute with 0.1 mL of distilled water.
Target Information
Secretory carrier membrane proteins (SCAMPs) are proteins that are components of post-Golgi membranes. These proteins are implicated to function in membrane trafficking. In fibroblasts, SCAMPs are concentrated in compartments that are involved in the recycling of cell surface receptors and endocytosis. In neurons, SCAMPs are associated with synaptic vesicles, secretion granules and transporter vesicles. SCAMPs are composed of four central transmembrane regions and a cytoplasmic tail. Of the five known SCAMPs, SCAMPs 1-3 contain cytoplasmic N-terminal regions with NPF repeats. NPF repeats are found to interact with EH domain proteins that function in budding of transport vesicles from the plasma membrane or the Golgi complex. SCAMPs 4 and 5 lack the N-terminal NPF repeats. SCAMPs 1-4 are all ubiquitously coexpressed while SCAMP 5 is only detectable in the brain. Studies show that SCAMP 5 is expressed late in development which is coincident with expansion of mature synapses.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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