Recombinant Human SorLA (aa 82-753) Protein, CF Summary
Ser82-Pro753, with a C-terminal 6-His tag
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 1 mg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||
When Recombinant Human SorLA (Catalog # 9880-LA) is immobilized at 2 µg/mL, Recombinant Human beta -NGF (Catalog # 256-GF) binds with an ED50 of 0.1-0.5 µg/mL.
2 μg/lane of Recombinant Human SorLA was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands 85 - 99 kDa.
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.
- Hampe, W. et al. (2000) J. Cell Sci. 113:4475.
- Rohe, M. et al. (2013) PLoS One. 8:72164.
- Glerup, S. et al. (2013) Cell Rep. 3:186.
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