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SAE0095

Sigma-Aldrich

Agrin Human

Recombinant, cell culture tested, expressed in HEK 293 cells

Sinónimos:

AGRN, Proteoglycan

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About This Item

UNSPSC Code:
12352202
NACRES:
NA.77

recombinant

expressed in HEK 293 cells

assay

≥95% (SDS-PAGE)

form

lyophilized powder

potency

attachment assay, measured by the ability of the immobilized agrin to support the adhesion of PC12 cells

technique(s)

cell culture | mammalian: suitable

suitability

endotoxin tested

shipped in

ambient

storage temp.

−20°C

General description

Agrin C-terminal human recombinant is expressed in human HEK 293 cells as a glycoprotein with a calculated molecular mass of 87 kDa (amino acids Ala1260-Pro2045, with an N-terminal His tag). The DTT-reduced protein migrates as a ∼100 kDa polypeptide on SDS-PAGE due to glycosylation. This protein is manufactured in human cells, with no serum. The human cells expression system allows human-like glycosylation and folding, and often supports higher bioactivity of the protein.

Biochem/physiol Actions

Agrin is a large extracellular heparan sulfate proteoglycan that is involved in the formation of the neuromuscular junction.
Agrin triggers the aggregation of acetylcholine receptors via the muscle-specific kinase (MuSK) and the low-density lipoprotein receptor-related protein 4 (Lrp4) receptor complex.
Agrin is required for the full regenerative capacity of neonatal mouse hearts.
Recombinant agrin has been shown in vitro to promote cardiomyocyte proliferation, as studied in mouse-induced and human-induced pluripotent stem cells. Recombinant agrin has been shown in vivo to promote cardiac regeneration, after induction of myocardial infarction in adult mice.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 2

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Xiu-Qing Fu et al.
Cell discovery, 6, 9-9 (2020-03-07)
During the development of mammalian neuromuscular junction (NMJ), the original supernumerary axon inputs are gradually eliminated, finally leaving each muscle fiber innervated by a single axon terminal. However, the molecular cues that mediate the elimination of redundant axon inputs remain

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