Cat: PA2000-3202

Recombinant Human LTB Protein,His

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Analytical Data

  • Gene name

    LTB

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    LTB;C14orf141;LTBP3;Latent-transforming growth factor beta-binding Protein 2

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q14767

  • Expression Region

    1-1821aa

  • AA Sequence

    MRPRTKARSPGRALRNPWRGFLPLTLALFVGAGHAQRDPVGRYEPAGGDANRLRRPGGSYPAAAAAKVYSLFREQDAPVAGLQPVERAQPGWGSPRRPTEAEARRPSRAQQSRRVQPPAQTRRSTPLGQQQPAPRTRAAPALPRLGTPQRSGAAPPTPPRGRLTGRNVCGGQCCPGWTTANSTNHCIKPVCEPPCQNRGSCSRPQLCVCRSGFRGARCEEVIPDEEFDPQNSRLAPRRWAERSPNLRRSSAAGEGTLARAQPPAPQSPPAPQSPPAGTLSGLSQTHPSQQHVGLSRTVRLHPTATASSQLSSNALPPGPGLEQRDGTQQAVPLEHPSSPWGLNLTEKIKKIKIVFTPTICKQTCARGHCANSCERGDTTTLYSQGGHGHDPKSGFRIYFCQIPCLNGGRCIGRDECWCPANSTGKFCHLPIPQPDREPPGRGSRPRALLEAPLKQSTFTLPLSNQLASVNPSLVKVHIHHPPEASVQIHQVAQVRGGVEEALVENSVETRPPPWLPASPGHSLWDSNNIPARSGEPPRPLPPAAPRPRGLLGRCYLNTVNGQCANPLLELTTQEDCCGSVGAFWGVTLCAPCPPRPASPVIENGQLECPQGYKRLNLTHCQDINECLTLGLCKDAECVNTRGSYLCTCRPGLMLDPSRSRCVSDKAISMLQGLCYRSLGPGTCTLPLAQRITKQICCCSRVGKAWGSECEKCPLPGTEAFREICPAGHGYTYASSDIRLSMRKAEEEELARPPREQGQRSSGALPGPAERQPLRVVTDTWLEAGTIPDKGDSQAGQVTTSVTHAPAWVTGNATTPPMPEQGIAEIQEEQVTPSTDVLVTLSTPGIDRCAAGATNVCGPGTCVNLPDGYRCVCSPGYQLHPSQAYCTDDNECLRDPCKGKGRCINRVGSYSCFCYPGYTLATSGATQECQDINECEQPGVCSGGQCTNTEGSYHCECDQGYIMVRKGHCQDINECRHPGTCPDGRCVNSPGSYTCLACEEGYRGQSGSCVDVNECLTPGVCAHGKCTNLEGSFRCSCEQGYEVTSDEKGCQDVDECASRASCPTGLCLNTEGSFACSACENGYWVNEDGTACEDLDECAFPGVCPSGVCTNTAGSFSCKDCDGGYRPSPLGDSCEDVDECEDPQSSCLGGECKNTVGSYQCLCPQGFQLANGTVCEDVNECMGEEHCAPHGECLNSHGSFFCLCAPGFVSAEGGTSCQDVDECATTDPCVGGHCVNTEGSFNCLCETGFQPSPESGECVDIDECEDYGDPVCGTWKCENSPGSYRCVLGCQPGFHMAPNGDCIDIDECANDTMCGSHGFCDNTDGSFRCLCDQGFEISPSGWDCVDVNECELMLAVCGAALCENVEGSFLCLCASDLEEYDAQEGHCRPRGAGGQSMSEAPTGDHAPAPTRMDCYSGQKGHAPCSSVLGRNTTQAECCCTQGASWGDACDLCPSEDSAEFSEICPSGKGYIPVEGAWTFGQTMYTDADECVIFGPGLCPNGRCLNTVPGYVCLCNPGFHYDASHKKCEDHDECQDLACENGECVNTEGSFHCFCSPPLTLDLSQQRCMNSTSSTEDLPDHDIHMDICWKKVTNDVCSEPLRGHRTTYTECCCQDGEAWSQQCALCPPRSSEVYAQLCNVARIEAEREAGVHFRPGYEYGPGPDDLHYSIYGPDGAPFYNYLGPEDTVPEPAFPNTAGHSADRTPILESPLQPSELQPHYVASHPEPPAGFEGLQAEECGILNGCENGRCVRVREGYTCDCFEGFQLDAAHMACVDVNECDDLNGPAVLCVHGYCENTEGSYRCHCSPGYVAEAGPPHCTAKE

  • Molecular Weight

    195 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

LTB (Lactobacillus transglutaminase-binding protein) is a protein that has garnered significant interest in the field of biotechnology due to its potential applications in food science, pharmaceuticals, and immunology. Research surrounding LTB primarily focuses on its role in protein interactions and its ability to form complexes with transglutaminases, enzymes that catalyze the cross-linking of proteins. This functionality positions LTB as a candidate for enhancing the texture and quality of food products, as well as for developing innovative drug delivery systems. Studies have suggested that LTB may play a critical role in microbial adhesion and colonization, making it an important target for understanding gut microbiota interactions and their influence on human health. Additionally, the exploration of LTB's immunogenic properties could lead to advancements in vaccine development, particularly in creating effective mucosal vaccines that target specific pathogens. The ongoing research into LTB not only aims to elucidate its biological mechanisms but also seeks to harness its properties for commercial applications, thus bridging the gap between fundamental science and practical solutions in health and nutrition.

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