Recombinant Human Agrin Protein, CF Summary
Product Specifications
Optimal dilutions should be determined by each laboratory for each application.
Ala1260-Pro2045, with an N-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
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.
6624-AG
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 300 μg/mL in PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Reconstitution Calculator
Background: Agrin
Agrin is a 400‑600 kDa heparan sulfate proteoglycan component of the extracellular matrix. The N-terminal half of human Agrin, which mediates ECM interactions, contains a Laminin-binding NtA domain, nine Kazal-type protease inhibitor domains, two Laminin EGF-like domains, and one SEA domain. The C‑terminal half contains four EGF-like repeats and three Laminin globular G domains. Rat Agrin lacks the NtA domain, and mouse and chick Agrin include the NtA domain only by the use of an alternate promoter. Additional isoforms are generated by alternate splicing at sites Y and Z in the C‑terminal half of rat Agrin (known as A and B, respectively in chick). Agrin isoforms that contain an insert at site Z (Z+ forms) are known as neural Agrin and are selectively produced by motoneurons. Other isoforms are known as muscle Agrin and are additionally expressed in non-neuronal tissues, particularly in basement membranes of the lung and kidney (1-3). This recombinant protein consists of the C‑terminal half of human Agrin corresponding to the Z- isoform of rat Agrin. It shares 60%, 78%, and 80% amino acid sequence identity with comparable regions of chick, mouse, and rat Agrin, respectively. The C‑terminal half of Z- and Z+ Agrin binds to alpha ‑Dystroglycan and mediates adhesion between motoneurons and myotubes at the neuromuscular junction (NMJ) (4-6). In contrast, only Z+ Agrin is effective at inducing clustering of the postsynaptic Acetylcholine Receptor (AChR) and presynaptic motoneuron differentiation (7, 8). Agrin-induced AChR clustering requires a myotube receptor complex that contains alpha ‑Dystroglycan, MuSK, and LRP4 (4, 9-11). Agrin exhibits many functions in addition to NMJ development. It is enriched in senile Alzheimer's disease plaques where it binds the A beta (1‑40) peptide and promotes amyloid fibril formation (12). It regulates neuronal excitability by binding and inhibiting the alpha 3 subunit of the neuronal Na/K ATPase (13). It functions as an epithelial cell attachment receptor for HIV-1 through interactions with the gp41 coat protein (14). During T cell activation, Agrin contributes to formation of the immunological synapse and regulates the threshold of T cell activation (15).
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Citations for Recombinant Human Agrin Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 9
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Molecular Analysis of a Congenital Myasthenic Syndrome Due to a Pathogenic Variant Affecting the C-Terminus of ColQ
Authors: Barbeau, S;Semprez, F;Dobbertin, A;Merriadec, L;Roussange, F;Eymard, B;Sternberg, D;Fournier, E;Karasoy, H;Martinat, C;Legay, C;
International journal of molecular sciences
Species: Human
Sample Types: Whole Cells
Applications: Differentiation -
Evaluation of Human-Induced Pluripotent Stem Cells Derived from a Patient with Schwartz-Jampel Syndrome Revealed Distinct Hyperexcitability in the Skeletal Muscles
Authors: Y Yamashita, S Nakada, K Nakamura, H Sakurai, K Ohno, T Goto, Y Mabuchi, C Akazawa, N Hattori, E Arikawa-Hi
Biomedicines, 2023-03-07;11(3):.
Species: Human, Mouse
Sample Types: Whole Cells
Applications: Cell Culture -
FUS-ALS hiPSC-derived astrocytes impair human motor units through both gain-of-toxicity and loss-of-support mechanisms
Authors: K Stoklund D, L Terrie, P Baatsen, A Kerstens, L De Swert, R Janky, N Corthout, P Masrori, P Van Damme, P Hyttel, M Meyer, L Thorrez, K Freude, L Van Den Bo
Molecular Neurodegeneration, 2023-01-18;18(1):5.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
The Hippo Pathway Effectors YAP/TAZ Are Essential for Mineralized Tissue Homeostasis in the Alveolar Bone/Periodontal Complex
Authors: M Pandya, G Gopinathan, C Tillberg, J Wang, X Luan, TGH Diekwisch
Journal of developmental biology, 2022-03-01;10(1):.
Species: Human
Sample Types: Whole Cells
Applications: Cell Culture -
Human motor units in microfluidic devices are impaired by FUS mutations and improved by HDAC6 inhibition
Authors: K Stoklund D, EN Krasnow, L Fumagalli, T Vandoorne, P Baatsen, A Kerstens, G Giacomazzi, B Pavie, E Rossaert, J Beckers, M Sampaolesi, P Van Damme, L Van Den Bo
Stem Cell Reports, 2021-04-22;0(0):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
iPSC-derived functional human neuromuscular junctions model the pathophysiology of neuromuscular diseases
Authors: CY Lin, M Yoshida, LT Li, A Ikenaka, S Oshima, K Nakagawa, H Sakurai, E Matsui, T Nakahata, MK Saito
JCI Insight, 2019-09-19;4(18):.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Collagen 18 and agrin are secreted by enteric neural crest cells to remodel their microenvironment and regulate their migration during ENS development
Authors: N Nagy, C Barad, R Hotta, S Bhave, E Arciero, D Dora, AM Goldstein
Development, 2018-05-08;0(0):.
Species: Chicken
Sample Types: Whole Cells
Applications: Bioassay -
Functional brain-specific microvessels from iPSC-derived human brain microvascular endothelial cells: the role of matrix composition on monolayer formation
Authors: ME Katt, RM Linville, LN Mayo, ZS Xu, PC Searson
Fluids Barriers CNS, 2018-02-20;15(1):7.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
The Different Binding Properties of Cultured Human Corneal Endothelial Cell Subpopulations to Descemet's Membrane Components
Invest Ophthalmol Vis Sci, 2016-09-01;57(11):4599-605.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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