Analytical Data
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Gene name
Agrin
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简介
Agrin is a heparan sulfate basal glycoprotein that is critical for the formation and maintenance of the neuromuscular junction (NMJ). It forms the AGRN-LRP4 receptor complex, activates MUSK and regulates gene transcription and AChR clusters in the postsynaptic membrane to form the NMJ. Agrin Protein, Human (1073a.a, CHO, His) is the recombinant human-derived Agrin protein, expressed by CHO , with C-6*His labeled tag.
- Application
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Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of U-87 MG human glioblastoma/astrocytoma cells. The ED50 for this effect is 195.7 ng/ml, corresponding to a specific activity is 5.11×10^3 units/mg. Measured by the ability of the immobilized protein to support the adhesion of U‑87 MG human glioblastoma/astrocytoma cells. The ED50 for this effect is 195.7ng/mL, corresponding to a specific activity is 5.11×103 units/mg.
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Alternative Names
agrin proteoglycan; Agrin; AGRN
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Species
Human
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Source
CHO
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O00468-1
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Expression Region
T30-R1102
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AA Sequence
TCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVER
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Protein Length
Full Length of Mature Agrin N-terminal 110 kDa subunit
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Molecular Weight
155.89 kDa
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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
Related Products
Protein Description
Agrin is a heparan sulfate proteoglycan that plays a pivotal role in the development of the neuromuscular junction (NMJ) by promoting the clustering of acetylcholine receptors on the postsynaptic muscle membrane. Initially identified for its function in synaptogenesis, recent studies have revealed Agrin's involvement in various cellular processes, including muscle repair and neuronal signaling. The significance of Agrin extends beyond NMJ formation, as it has been implicated in neuromuscular diseases and conditions such as myasthenia gravis and congenital myasthenic syndromes. Given its critical functions, researchers have focused on characterizing Agrin's structure, post-translational modifications, and the specific mechanisms by which it influences cellular signaling pathways. Recombinant Agrin proteins are being developed to investigate their mechanistic roles and therapeutic potential, particularly in restoring NMJ function in disease models. This research aims to enhance our understanding of synaptic disorders and pave the way for novel therapeutic strategies that leverage the properties of Agrin to improve muscle function and neuromuscular health. As such, the study of Agrin not only encompasses fundamental molecular biology but also holds significant therapeutic promise in the context of neuromuscular diseases.
