Analytical Data
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Gene name
Agrin
- Application
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Alternative Names
Agrin Proteoglycan
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00468
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Expression Region
Leu1856~Pro2045
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Molecular Weight
27kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Agrin is a vital extracellular matrix protein that plays a critical role in the formation and maintenance of neuromuscular junctions (NMJs). Initially identified for its function in synaptic differentiation, Agrin is produced primarily by motoneurons and is secreted into the synaptic cleft, where it binds to specific receptors on muscle cells, initiating signaling pathways that lead to the clustering of acetylcholine receptors (AChRs) at the NMJ. Given its essential function in neuromuscular signaling, disruptions in Agrin signaling have been implicated in various neuromuscular disorders, including congenital myasthenic syndromes and certain forms of muscular dystrophy. Recent research has focused on the recombinant production of Agrin, which allows for detailed studies of its structure-function relationships, the investigation of its signaling mechanisms, and the potential therapeutic applications in muscle regeneration and nerve repair. The development of recombinant Agrin also facilitates the study of its interactions with other molecules in the extracellular matrix and its role in synaptic plasticity, potentially leading to new insights into NMJ pathology and novel treatment strategies for neuromuscular diseases. Understanding Agrin's multifaceted roles at the NMJ not only advances our knowledge of muscle biology and nerve-muscle communication but also opens avenues for innovative therapeutic approaches that address debilitating neuromuscular conditions.
