Recombinant Human Agrin (AGRN) Protein (His)

Name: Recombinant Human Agrin (AGRN) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00594P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Agrin (AGRN) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O00468
Target Symbol	AGRN
Synonyms	(C90)(C22)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His
Target Protein Sequence	VDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPC
Expression Range	1868-2065aa
Protein Length	Partial
Mol. Weight	27.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain.; transmembrane form that is the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; Isoform 1, isoform 4 and isoform 5: neuron-specific (z+) isoforms that contain C-terminal insertions of 8-19 AA are potent activators of AChR clustering. Isoform 5, agrin (z+8), containing the 8-AA insert, forms a receptor complex in myotubules containing the neuronal AGRN, the muscle-specific kinase MUSK and LRP4, a member of the LDL receptor family. The splicing factors, NOVA1 and NOVA2, regulate AGRN splicing and production of the 'z' isoforms.; Isoform 3 and isoform 6: lack any 'z' insert, are muscle-specific and may be involved in endothelial cell differentiation.; is involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.; this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.
Subcellular Location	[Isoform 1]: Secreted, extracellular space, extracellular matrix.; [Isoform 2]: Cell junction, synapse. Cell membrane; Single-pass type II membrane protein.
Database References	HGNC: 329 OMIM: 103320 KEGG: hsa:375790 STRING: 9606.ENSP00000368678 UniGene: PMID: 29351440 The presence of agrin at locations with particular importance for the growth and stability of atherosclerotic plaques renders this molecule strategically positioned to influence plaque development and vulnerability PMID: 29405249 C-terminal agrin fragment levels predict acute kidney injury after acute myocardial infarction. PMID: 28646861 Agrin promotes oncogenesis through YAP-dependent transcription. PMID: 28273460 Agrin strongly promotes chondrocyte differentiation and cartilage formation in vivo. PMID: 26290588 Knockdown of agrin and perlecan promoted a decrease on cell migration and adhesion, and on resistance of cells to cisplatin. PMID: 25506919 Among 42 hip fractured patients (age 83.7+/-8.6 years, 76.2% women), sarcopenia was diagnosed in 7 individuals (16.7%). Serum C-terminal agrin fragment (CAF) levels were significantly higher in sarcopenic relative to non-sarcopenic patients. PMID: 25304331 In patients suffering from severe sepsis and septic shock, serum levels of C-terminal agrin fragment were significantly associated with kidney function and the need for renal replacement therapy and were not influenced by severe septic conditions. PMID: 25807640 MuSK myasthenia gravis IgG4 disrupts the interaction of LRP4 with MuSK but both IgG4 and IgG1-3 can disperse preformed agrin-independent AChR clusters PMID: 24244707 these observations indicate that agrin is another autoantigen in patients with MG and agrin autoantibodies may be pathogenic through inhibition of agrin/LRP4/MuSK signaling at the NMJ. PMID: 24632822 Five new recessive mutations in the gene encoding agrin are identified in patients with congenital myasthenic syndrome. PMID: 24951643 study identifies a spontaneous agrin mutation that reduces the ability of z+ agrin to activate MuSK and induce AChR clustering; this results in a severe congenital myasthenic syndrome in the patient, with both pre- and postsynaptic defects at the neuromuscular junction PMID: 22205389 Dynamics of expression patterns of agrin in human glioblastoma PMID: 22307776 In contrast to wild-type neurons which form synapses and survive for prolonged periods, agrin-deficient neurons do not mature and are rapidly eliminated in the transgenic olfactory bulb. PMID: 22423096 Agrin immunohistochemistry may facilitate determination of primary versus metastatic origin in problematic liver cancer cases. PMID: 20471664 different regions within the agrin protein are responsible for synapse formation at the neuromuscular junction and for process formation in central nervous system neurons PMID: 19940118 Agrin, a heparan sulfate proteoglycan, is a component of the basal lamina of BBB microvessels, and growing evidence suggests that it may be important for the maintenance of the BBB. PMID: 12070669 acts at the nerve-muscle synapse in the glomerular basal membrane and on T-lymphocytes PMID: 12073527 evidence for additional functions of agrin during axonal growth, establishment of the blood-brain barrier, and Alzheimer's disease is accumulating--REVIEW PMID: 12270958 Thus, an agrin/MuSK complex may form part of a motor neuron stop signal involved in "reverse signaling" to the motor neuron. PMID: 15691710 in the NtA-laminin complex, conserved amino acids in the gamma 1 chain are prerequisite for the binding to agrin PMID: 15694127 agrin has a role in binding alpha-synuclein and modulating alpha-synuclein fibrillation PMID: 16037493 In human sperm an agrin isoform with a short NH2-terminus (agrinSN) localized in the posterior post-acrosomal, neck, and flagellar mid-piece regions. PMID: 16487930 agrin might play an important role in neoangiogenesis in human HCC, being a part of the newly formed vasculature. In CC, however, agrin might be involved in tumor progression PMID: 17640714 The agrin expression in human T cells is regulated by cell activation and IFN-alpha, and may have an important function during cell activation with potential implications for autoimmunity. PMID: 18025246 study concludes that Abeta can modulate the cellular expression of agrin and glypican-1, which may contribute to the accumulation of these heparan sulfate proteoglycans in Alzheimer's disease lesions PMID: 19166823 agrin facilitates the discrimination of benign and malignant hepatocellular lesions PMID: 19194276 The agrin mutation does not interfere with its ability to induce postsynaptic structures but that it dramatically perturbs the maintenance of the neuromuscular junction. PMID: 19631309 Observational study of gene-disease association. (HuGE Navigator) PMID: 19598235

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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