Recombinant Human MuSK Fc Chimera Avi-tag Protein, CF Summary
Accession # O15146.1
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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 with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Biotinylated Recombinant Human MuSK Fc Chimera Avi-tag Protein (Catalog # AVI9810) is immobilized onto a Streptavidin coated plate (CP004) at 2 µg/mL (100 µL/well), in the presence of Recombinant Human Agrin (6624-AG), it binds to Recombinant Human LRP-4 (5948-LR) with an ED50 of 0.600-4.80 ng/mL.
2 μg/lane of Biotinylated Recombinant Human MuSK Fc Chimera Avi-tag Protein (Catalog # AVI9810) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 87-102 kDa and 170-200 kDa, respectively.
MuSK (muscle-specific kinase) is a 100 kDa type I transmembrane (TM) protein belonging to the receptor tyrosine kinase family (1). It contains a 472 aa extracellular domain (ECD), a 21 aa transmembrane domain, and a 353 cytoplasmic domain (1). Within the ECD, Human MuSK shares 91% and 92% aa sequence identity with mouse MuSK and rat MuSK, respectively. It is found in the postsynaptic membrane of skeletal muscle motor endplates (2). Human MuSK has multiple isoforms. One contains deletions at residues 307‑394 and 454‑461, while a second is a short soluble form that contains residues 120‑209 plus a unique 24 aa C‑terminal tail (3). MuSK binds the heparin sulfate proteoglycan agrin to promote acetylcholine receptor clustering. It has also been found to bind with low-density lipoprotein receptor-related protein 4 (LRP4) (4), Wnt ligands (5), biglycan (6), and ColQ (7). Recent studies have showed that MuSK does not bind agrin directly, but enhanced the MuSK-LRP4 interaction (7, 8). When Agrin binds to the N-Terminal region of LRP4, this promotes the association of LRP4 and MuSK, which then stimulates MuSK kinase activity (9, 10). Our Avi-tag Biotinylated human MUSK Fc Chimera features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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- Burden, S.J. et al. (2017) CSH Perspectives Biol. 5:a009167.
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