Cat: IPD-X27089

Recombinant Others Heparinase II Protein,His

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Analytical Data

  • Gene name

    Heparinase II

  • 简介

    Heparinase II protein is an enzyme that cleaves heparin and heparan sulfate glycosaminoglycans using a beta elimination mechanism. Specifically, it cleaves heparin at the α-D-GlcNp2S6S(1->4) α-L-IdoAp2S site and at the α-D-GlcNp2Ac(or 2S)6OH(1->4)beta-D-GlcAp position Site of cleavage of heparan sulfate. Heparinase II Protein, P. heparinus (His) is the recombinant Heparinase II protein, expressed by E. coli , with N-His labeled tag.

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Heparinase II

  • Species

    Others

  • Source

    E. coli

  • Tag

    N-6*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    C6XZB6

  • Expression Region

    Q26-R772

  • AA Sequence

    QTKADVVWKDVDGVSMPIPPKTHPRLYLREQQVPDLKNRMNDPKLKKVWADMIKMQEDWKPADIPEVKDFRFYFNQKGLTVRVELMALNYLMTKDPKVGREAITSIIDTLETATFKPAGDISRGIGLFMVTGAIVYDWCYDQLKPEEKTRFVKAFVRLAKMLECGYPPVKDKSIVGHASEWMIMRDLLSVGIAIYDEFPEMYNLAAGRFFKEHLVARNWFYPSHNYHQGMSYLNVRFTNDLFALWILDRMGAGNVFNPGQQFILYDAIYKRRPDGQILAGGDVDYSRKKPKYYTMPALLAGSYYKDEYLNYEFLKDPNVEPHCKLFEFLWRDTQLGSRKPDDLPLSRYSGSPFGWMIARTGWGPESVIAEMKVNEYSFLNHQHQDAGAFQIYYKGPLAIDAGSYTGSSGGYNSPHNKNFFKRTIAHNSLLIYDPKETFSSSGYGGSDHTDFAANDGGQRLPGKGWIAPRDLKEMLAGDFRTGKILAQGFGPDNQTPDYTYLKGDITAAYSAKVKEVKRSFLFLNLKDAKVPAAMIVFDKVVASNPDFKKFWLLHSIEQPEIKGNQITIKRTKNGDSGMLVNTALLPDAANSNITSIGGKGKDFWVFGTNYTNDPKPGTDEALERGEWRVEITPKKAAAEDYYLNVIQIADNTQQKLHEVKRIDGDKVVGVQLADRIVTFSKTSETVDRPFGFSVVGKGTFKFVMTDLLPGTWQVLKDGKILYPALSAKGDDGALYFEGTEGTYRFLR

  • Protein Length

    Full Length of Mature Protein

  • Molecular Weight

    85 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

Heparinase II is an important enzyme derived from the bacterium Flavobacterium heparinum, known for its ability to degrade heparin and heparan sulfate, which are glycosaminoglycans involved in various physiological processes, including cell signaling, coagulation, and wound healing. The significance of Heparinase II extends to its potential therapeutic applications, particularly in anticoagulation therapy and the development of novel biomaterials. Given its specificity and effectiveness in breaking down glycosaminoglycans, researchers have focused on producing recombinant forms of Heparinase II to enhance its yield, stability, and functional properties. The recombinant protein production enables detailed studies of the enzyme's mechanism, structure-function relationships, and interactions with various cellular components. Additionally, the study of Heparinase II and its recombinant variants opens new avenues for drug delivery systems and tissue engineering applications, as it can facilitate the release of bound growth factors and enhance tissue regeneration. Understanding the biochemical properties and enzymatic activity of recombinant Heparinase II could lead to significant advancements in various biomedical fields, making it a topic of considerable interest in modern research.

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