When Recombinant Human SorLA His-tag Protein (Catalog # 11083-LA) is coated at 0.250 μg/mL (100 μL/well), it binds to Recombinant Human PDGF-BB (220-BB). The ED50 for this binding is 2.00‑30.0 ng/mL.
2 μg/lane of Recombinant Human SorLA His-tag Protein (Catalog # 11083-LA) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at ...read more
Recombinant Human SorLA His-tag Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human SorLA His-tag Protein is coated at 0.250 μg/mL (100 μL/well), it binds to Recombinant Human PDGF-BB
(Catalog #
220-BB). The ED50 for this binding is 2.00-30.0 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human SorLA protein Ser82-Asp2135, with a C-terminal 6-His tag
>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
Bioactivity
Theoretical MW
232 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
270-345 kDa, under reducing conditions.
Publications
Read Publication using 11083-LA in the following applications:
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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 1.00 mg/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 SorLA His-tag Protein, CF
C11orf32
chromosome 11 open reading frame 32
FLJ21930
FLJ39258
gp250
Low-density lipoprotein receptor relative with 11 ligand-binding repeats
LR11
LR11LDLR relative with 11 ligand-binding repeats
LRP9
mosaic protein LR11
SORL1
SorLA
SorLA-1SORLA
sortilin-related receptor
sortilin-related receptor, L(DLR class) A repeats containing
sortilin-related receptor, L(DLR class) A repeats-containing
Sorting protein-related receptor containing LDLR class A repeats
Background
SorLA
(sortilin-related receptor, LDLR class A repeats-containing), also called LR11
or SORL1, is a 250 kDa type I transmembrane glycoprotein of the Sortilin family
of Vps10p-domain receptors (1, 2). SorLA is found in both intracellular and
surface membranes in the central nervous system, and mediates trafficking of
proteins such as the amyloid precursor protein (APP) (3-5). The 2214 amino acid
(aa) human SorLA precursor includes a 28 aa signal sequence and a 53 aa furin-cleaved
propeptide. The mature SorLA contains a vacuolar
protein sorting 10 protein (Vps10p) homology domain, beta -propeller and epidermal
growth factor (EGF) domains, a cluster of 11 complement-type repeat domains,
six fibronectin type III repeats, a single transmembrane domain (TM), and a
cytoplasmic domain (CT) (1, 6-7). Human SorLA shares 93% and 92% aa sequence
identity with mouse and rat SorLA, respectively. SorLA is mainly expressed in
nervous system, but is also found in non-neuronal tissues (8). Upon truncation,
SorLA is able to bind multiple ligands among which are RAP, apolipoprotein E,
and lipoprotein lipase, and facilitate both their endocytosis and sorting (1).
The expression, translocation, and ectodomain shedding were shown to be induced
by its ligand head activator peptide (HA) (9). SorLA has also been shown to be important in
Alzheimer's disease through multiple functions, but especially through its
ability to bind Amyloid Precursor Protein (4).
It is involved in TrkB receptor and GFRa1 trafficking and further
enhancement of BDNF and GDNF functions respectively (10, 11).
Jacobsen, L. et al. (2001) J. Biol. Chem. 276:22788.
Wang, X. et al. (2011) Protein Expr. Purif. 77:224.
Small, S.A. and S. Gandy (2006) Neuron. 52:15.
Andersen, O.M. et al. (2005) Proc. Natl. Acad. Sci. U. S. A. 102:13461.
Willnow, T.E. et al. (2008) Nat. Rev. Neurosci. 9:899.
Herz J. (2001) Neuron 29:571.
Yamazaki H. et al. (1996) J. Biol. Chem. 271:24761.
Jacobsen L. et al. (1996) J. Biol. Chem. 271:31379.
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