Recombinant Human APLP-1 Protein, CF Summary
Details of Functionality |
Bioassay data are not available. |
Source |
Mouse myeloma cell line, NS0-derived human APLP-1 protein Gln34-Glu580, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Gln34 (blocked) |
Protein/Peptide Type |
Innovator Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
62 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
74-89 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human APLP-1 Protein, CF
Background
Amyloid Precursor-like
Proteins (APLPs) are members of the amyloid precursor protein (APP) superfamily
of transmembrane proteins. APLP-1, APLP-2, and APP share highly homologous amino
acid sequences, except that APLPs lack the beta -amyloid domain derived by proteolytic
processing from APP (1). APLP-1 is expressed post-synaptically in cortical
neurons (2). APLP-1 is post-translationally modified by N-glycosylation and
displays an apparent molecular mass of 80-90 kDa in reducing SDS-PAGE (3). Similar
to APP and APLP-2, APLP-1 is susceptible to cleavage by MMPs and secretases,
generating multiple fragments from the extracellular and intracellular domains (4).
These include peptides similar to the amyloidogenic A beta peptides and a
cytoplasmic fragment that associates with Fe65 family proteins and functions as
a transcriptional activator (4). The extracellular domain contains heparin and
collagen binding regions. human APLP-1 shares 88% and 86% aa sequence identity
with mouse and rat APLP-1, respectively.
-
Suzuki, T. et al. (1997) Biochemistry 36:4643.
- Kim, T. W. et al. (1995) Brain Res. Mol. Brain Res. 32:36.
- Paliga, K. et al. (1997) Eur. J. Biochem. 250:354.
- Scheinfeld, M. H. et al. (2002) J. Biol. Chem. 277:44195.
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