Recombinant Human LDL Receptor

Low-density lipoprotein receptor-related protein 4, LRP-4, Multiple epidermal growth factor-like domains 7, LRP4, KIAA0816, LRP10, MEGF7.

LRP4 encodes a part of the low-density lipoprotein receptor-related protein family, which comprises of many evolutionarily conserved transmembrane proteins. LRP4 mediates SOST-dependent inhibition of bone formation. LRP4 takes part in the formation and the maintenance of the neuromuscular junction which is the synapse between skeletal muscle and motor neuron. LRP4 plays a role as a specific facilitator of SOST-mediated inhibition of Wnt signaling.

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).

HEK293 Cells.

Filtered White lyophilized (freeze-dried) powder.

LRP4 filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in PBS, 5% (w/v) trehalose pH 7.5.

It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely

Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

Greater than 95.0% as determined by SDS-PAGE.

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

SDS

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