Recombinant Cynomolgus Monkey MuSK Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. In
the presence of Recombinant Human Agrin
(Catalog #
6624-AG), immobilized Recombinant
Cynomolgus Monkey MuSK Fc Chimera
(Catalog # 11122-MK) at 0.5 µg/mL (100
µL/well) binds Recombinant Human LRP-4
(Catalog #
5948-LR) with an ED 50
of 10.0-80.0 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey MuSK protein Cyno MuSK (Leu24-Thr495) Accession # XP_005581150.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
N-terminal Sequence |
Leu24 |
Structure / Form |
Disulfide-linked homodimer. Biotinylated via Avi-tag. |
Protein/Peptide Type |
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 |
78 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 |
85-105 kDa, under 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 with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 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 Cynomolgus Monkey MuSK Fc Chimera Protein, CF
Background
Muscle-specific kinase (MuSK), also known as muscle skeletal receptor
tyrosine-protein kinase, is a single-pass transmembrane protein belonging to
the protein kinase superfamily (1). Cynomolgus MuSK consists of an extracellular domain (ECD) with 3 immunoglobulin-like
domains and a cysteine-rich domain (CRD), a transmembrane domain, and a
cytoplasmic domain with a tyrosine kinase domain (2). Within the mature ECD,
cynomolgus MuSK shares 99% and 91% amino acid sequence identity with human and
mouse MuSK, respectively. Alternative
splicing of MuSK results in multiple isoforms which could result in altered
properties and functions (3, 4). MuSK
is expressed by skeletal muscle cells and excitatory neurons in the central
nervous system (CNS) (1, 2). MuSK is essential for neuromuscular synapse formation
and activation of the MuSK signaling cascade is critical for proper signaling
between motor neurons and skeletal muscle (1-4). Once activated, MuSK
stimulates the pathways that facilitate transcription of genes which encode
synaptic proteins in muscle, activate retrograde signaling which promotes
presynaptic differentiation, and cluster and anchor acetylcholine receptors
(AChRs) (1, 5). Low-density lipoprotein receptor-related protein-4 (Lrp4), is
the ligand for MuSK, and its binding affinity is potentiated by agrin (3). Mutant
mice lacking agrin, MuSK, and Lrp4 fail to form neuromuscular junctions (NMJ)
and subsequently died at birth due to respiratory failure (2, 3). In the
presence of mutations which impair MuSK kinase activity or downstream signaling
from MuSK, synapses become both structurally and functionally defective, leading
to congenital myasthenia (6). The autoimmune disease myasthenia gravis is
another neuromuscular disease caused by autoantibodies to AChRs, MuSK or Lrp4 (6). Our Avi-tag Biotinylated MuSK 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
- Burden, S.J. et al. (2013) CSH Perspectives Bio. 5(5).
- Hubbard, S.R. and Gnanasambandan, K. (2013) Biochem Biophys Acta. 1834(10):2166.
- Nasrin, F. et al. (2014) Sci. Rep. 4:6841.
- Kuehn, R. et al. (2005) Gene 360:83.
- Camurdanoglu, B.Z. et al. (2016) Sci. Rep. 6:33583.
- Herbst, R. (2020) Neurosci. Lett. (2020) 716:134676.
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