HEK293 Cells.
Low-density lipoprotein receptor-related protein 4, LRP-4, Multiple epidermal growth factor-like domains 7, LRP4, KIAA0816, LRP10, MEGF7.
Greater than 95.0% as determined by SDS-PAGE.
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LRP4 Human Recombinant is a single, glycosylated polypeptide chain containing 1719 amino acids (21-1725a.a) and having a molecular mass of 191.6kDa (calculated). LRP4 is fused to a 14 a.a His tag (2 a.a on N-terminal and 12 a.a on C-terminal).
LRP4, a member of the low-density lipoprotein receptor-related protein family, plays a crucial role in bone formation and neuromuscular junction development. This family consists of numerous evolutionarily conserved transmembrane proteins. LRP4 facilitates SOST-dependent inhibition of bone formation and is involved in the formation and maintenance of the neuromuscular junction, the synapse between skeletal muscle and motor neurons. Furthermore, it acts as a specific facilitator of SOST-mediated inhibition of Wnt signaling.
Recombinant human LRP4 is a single, glycosylated polypeptide chain with a molecular weight of 191.6 kDa (calculated). It comprises 1719 amino acids, spanning from amino acid residues 21 to 1725a.a. The protein is fused to a 14 amino acid His tag, with 2 amino acids on the N-terminal and 12 amino acids on the C-terminal.
LRP4 is supplied as a lyophilized powder, having been filtered through a 0.4 μm filter. The protein was initially in a 0.5 mg/mL solution of PBS (pH 7.5) containing 5% (w/v) trehalose before lyophilization.
To prepare a working stock solution, it is recommended to add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5 mg/mL. Allow the pellet to dissolve completely.
The purity of LRP4 is determined to be greater than 95.0% using SDS-PAGE analysis.
Low-density lipoprotein receptor-related protein 4, LRP-4, Multiple epidermal growth factor-like domains 7, LRP4, KIAA0816, LRP10, MEGF7.
HEK293 Cells.
ASSSPECACG RSHFTCAVSA LGECTCIPAQ WQCDGDNDCG DHSDEDGCIL PTCSPLDFHC DNGKCIRRSW VCDGDNDCED DSDEQDCPPR ECEEDEFPCQ NGYCIRSLWH CDGDNDCGDN SDEQCDMRKC SDKEFRCSDGS CIAEHWYCDG DTDCKDGSDE ENCPSAVPAP PCNLEEFQCA YGRCILDIYH CDGDDDCGDW SDESDCSSHQ PCRSGEFMCD SGLCINAGWRC DGDADCDDQS DERNCTTSMCT AEQFRCHSGR CVRLSWRCDG EDDCADNSDE ENCENTGSPQ CALDQFLCWN GRCIGQRKLC NGVNDCGDNS DESPQQNCRP RTGEENCNVN NGGCAQKCQM VRGAVQCTCH TGYRLTEDGH TCQDVNECAE EGYCSQGCTN SEGAFQCWCE TGYELRPDRR SCKALGPEPV LLFANRIDIR QVLPHRSEYT LLLNNLENAIA LDFHHRRELV FWSDVTLDRI LRANLNGSNV EEVVSTGLES PGGLAVDWVH DKLYWTDSGTSR IEVANLDGAHR KVLLWQNLEK PRAIALHPME GTIYWTDWGN TPRIEASSMD GSGRRIIADTHL FWPNGLTIDYAG RRMYWVDAKHHVI ERANLDGSHRK AVISQGLPHPFA ITVFEDSLYWTDW HTKSINSANKFTG KNQEIIRNKLHFPM DIHTLHPQRQPAGK NRCGDNNGGCTHLC LPSGQNYTCACPTG FRKISSHACAQ SLDKFLLFAR RMDIRRISFD TEDLSDDVIPL ADVRSAVALDW DSRDDHVYWT DVSTDTISRAKW DGTGQEVVVDT SLESPAGLAID WVTNKLYWTD AGTDRIEVAN TDGSMRTVLIW ENLDRPRDIVV EPMGGYMYWTDW GASPKIERAGM DASGRQVIISS NLTWPNGLAIDY GSQRLYWADAG MKTIEFAGLD GSKRKVLIGSQL PHPFGLTLYGE RIYWTDWQTKS IQSADRLTGLD RETLQENLEN LMDIHVFHRRR PPVSTPCAMEN GGCSHLCLRS PNPSGFSCTCP TGINLLSDGKT CSPGMNSFLI FARRIDIRMVSL DIPYFADVVVP INITMKNTIA VGVDPQEGKV YWSDSTLHRI SRANLDGSQH EDIITTGLQT TDGLAVDAIG RKVYWTDTGT NRIEVGNLDG SMRKVLVWQNL DSPRAIVLYH EMGFMYWTDWG ENAKLERSGM DGSDRAVLIN NNLGWPNGLT VDKASSQLLWA DAHTERIEAA DLNGANRHTL VSPVQHPYGLTL LDSYIYWTDW QTRSIHRADK GTGSNVILVR SNLPGLMDMQ AVDRAQPLGF NKCGSRNGGC SHLCLPRPSG FSCACPTGIQ LKGDGKTCDPS PETYLLFSSR GSIRRISLDT SDHTDVHVPV PELNNVISLDY DSVDGKVYYTD VFLDVIRRAD LNGSNMETVI GRGLKTTDGL AVDWVARNLYW TDTGRNTIEASR LDGSCRKVLINN SLDEPRAIAVF PRKGYLFWTDW GHIAKIERANLD GSERKVLINTDL GWPNGLTLDYDTR RIYWVDAHLDRI ESADLNGKLRQ VLVGHVSHPFAL TQQDRWIYWTD WQTKSIQRVD KYSGRNKETVL ANVEGLMDII VVSPQRQTGTN ACGVNNGGCT HLCFARASDFVC ACPDEPDSQPC SLVPGLVPPA PRATGMSEKS PVLPNTPPTT LYSSTTRTRT SLEEVEGRCS ERDARLGLCA RSNDAVPAAP GEGLHISKLH HHHHHHHHH
LRP4 is a type I membrane protein with an approximate molecular weight of 220-270 kDa . It is known to interact with several ligands, including WISE, apoE, MuSK, and neuronal Agrin . One of the key functions of LRP4 is its role in the formation and maintenance of the neuromuscular junction (NMJ), where it forms a complex with MuSK and binds neural agrin to stimulate MuSK kinase activity . This interaction is essential for the proper differentiation and clustering of acetylcholine receptors at the postsynaptic membrane .
LRP4 is involved in various developmental processes, including the formation of bones, teeth, mammary placodes, and hair follicles . It is also crucial for the proper development and morphogenesis of limbs, ectodermal organs, lungs, and kidneys . In the context of the NMJ, LRP4 is required for both presynaptic and postsynaptic differentiation, and its absence can lead to severe neuromuscular defects .
Mutations in the LRP4 gene have been associated with several human diseases, including myasthenia syndromes and other neuromuscular disorders . Research has shown that LRP4 is required during the earliest events in postsynaptic NMJ formation and acts in the early, nerve-independent steps of NMJ assembly . This makes LRP4 a potential target for therapeutic interventions in neuromuscular diseases.
Recombinant human LRP4 is produced using advanced biotechnological methods to study its structure, function, and interactions in various biological systems . This recombinant protein is used in research to understand the molecular mechanisms underlying its role in development and disease, as well as to develop potential therapeutic strategies for conditions associated with LRP4 dysfunction .