Agrin Rat
Sf9, Baculovirus cells.
Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR
Greater than 90.0% as determined by SDS-PAGE.
Description
Agrin Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 766 amino acids (997-1753 a.a.) and having a molecular mass of 82.5kDa.
Agrin is fused to a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Agrin, Agrn, C90, C22, Agrin N-terminal 110 kDa subunit, Agrin C-terminal 110 kDa subunit, Agrin C-terminal 90 kDa fragment, Agrin C-terminal 22 kDa fragment, AGR
Sf9, Baculovirus cells.
ADPSCYNSPL GCCSDGKTPS LDSEGSNCPA TKAFQGVLEL EGVEGQELFY TPEMADPKSE LFGETARSIE STLDDLFRNS DVKKDFWSVR LRELGPGKLV RAIVDVHFDP TTAFQASDVG QALLRQIQVS RPWALAVRRP LQEHVRFLDF DWFPTFFTGA ATGTTAAMAT ARATTVSRLP ASSVTPRVYP SHTSRPVGRT TAPPTTRRPP TTATNMDRPR TPGHQQPSKS CDSQPCLHGG
TCQDQDSGKG FTCSCTAGRG GSVCEKVQPP SMPAFKGHSF LAFPTLRAYH TLRLALEFRA LETEGLLLYN GNARGKDFLA LALLDGRVQF RFDTGSGPAV LTSLVPVEPG RWHRLELSRH WRQGTLSVDG ETPVVGESPS GTDGLNLDTN LYVGGIPEEQ VAMVLDRTSV GVGLKGCIRM LDINNQQLEL SDWQRAAVQS SGVGECGDHP CLPNPCHGGA LCQALEAGMF LCQCPPGRFG PTCADEKSPC QPNPCHGAAP CRVLSSGGAK CECPLGRSGT FCQTVLETAG SRPFLADFNG FSYLELKGLH TFERDLGEKM ALEMVFLARG PSGLLLYNGQ KTDGKGDFVS LALHNRHLEF CYDLGKGAAV IRSKEPIALG TWVRVFLERN GRKGALQVGD GPRVLGESPK SRKVPHTMLN LKEPLYIGGA PDFSKLARGA AVSSGFSGVI QLVSLRGHQL LTQEHVLRAV DVSPFADHPC TQALGNPCLN GGSCVPREAT YECLCPGGFS GLHCEKGLVE HHHHHH
Product Science Overview
Agrin is a high-molecular-weight protein, typically ranging from 400 to 600 kDa . The N-terminal half of rat agrin contains several important domains that mediate its interactions with the ECM and other proteins:
- Nine Kazal-type protease inhibitor domains: These domains are involved in inhibiting proteases, which are enzymes that break down proteins.
- Two Laminin EGF-like domains: These domains are similar to epidermal growth factor (EGF) and are involved in binding to laminin, a major component of the basal lamina.
- One SEA domain: This domain is involved in protein-protein interactions.
The C-terminal portion of agrin contains three laminin G-like (LG) domains, which are crucial for its function at the NMJ . The LG1 and LG2 domains are essential for binding to α-dystroglycan (Dag1), while the LG3 domain is necessary for binding to the muscle-specific kinase (MuSK) and low-density lipoprotein receptor-related protein 4 (Lrp4) receptor complex .
Agrin is secreted by motor neurons and deposited into the synaptic basal lamina at the NMJ. It binds to receptors on the muscle cell surface, including MuSK and Lrp4, triggering a signaling cascade that leads to the clustering of AChRs . This process is vital for the proper transmission of nerve impulses to muscle fibers, enabling muscle contraction.
In addition to its role at the NMJ, agrin has been shown to have functions in other tissues, including the central nervous system and the heart. For example, agrin has been implicated in promoting cardiac repair and regeneration following myocardial infarction (MI) by enhancing angiogenesis, reducing fibrosis, and improving heart function .
Recombinant rat agrin is produced using baculovirus expression systems in insect cells (Spodoptera frugiperda, Sf21). The recombinant protein typically includes an N-terminal Met and a 6-His tag for purification purposes . The protein is purified to a high degree of purity (>90%) and is tested for its ability to induce AChR clustering on myotubes differentiated from C2C12 mouse myoblast cells .
Recombinant agrin is used extensively in research to study its role in NMJ formation and maintenance, as well as its potential therapeutic applications. For instance, studies have demonstrated that recombinant agrin can improve cardiac repair in animal models of MI, suggesting its potential as a therapeutic agent for heart disease .
