Recombinant HPSE protein (His tag)

Recombinant HPSE protein (His tag)

Cat.#: 548540

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Product Information

  • Product Name
    Recombinant HPSE protein (His tag)
  • Documents
  • Description

    Recombinant Human Heparanase (EC 3.2.1.166) Fragment (residues 158-543) is a high-purity, soluble protein designed for structural and biochemical studies. This 386-amino acid fragment retains key functional regions, offering researchers a stable tool to investigate heparan sulfate cleavage, extracellular matrix remodeling, and roles in metastasis, inflammation, and angiogenesis.

    Heparanase (HPSE) is an endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs), facilitating extracellular matrix degradation and remodeling under acidic conditions. It plays critical roles in tumor invasion, cell migration, wound healing, and inflammation by enhancing shedding of syndecans, promoting angiogenesis via VEGF activation, and acting as a procoagulant. Non-enzymatically, it supports cell adhesion and AKT1/PKB-mediated cell mobility. The full-length protein is synthesized as a proenzyme, secreted via Golgi vesicles, and processed in lysosomes into active 8 kDa and 50 kDa subunits, with localization in lysosomal membranes, endosomes, and occasionally the nucleus or cell surface. Its association with lipid rafts and HSPGs underscores its importance in pathological and physiological processes.

  • Protein name
    Heparanase
  • Uniprot ID
    Q9Y251
  • Gene Name
    HPSE; HEP; HPA; HPA1; HPR1; HPSE1; HSE1
  • Source/Expression Host
    E. coli
  • Expression Plasmid/cDNA
    DNA encoding 158-543 aa (Q9Y251) were fused with 6His tag.
  • Protein Species
    Human
  • Molecular weight
    Predictes a molecular mass of 45.04 kDa. In SDS-PAGE under reducing conditions, it migrates as an approximately 45 kDa band.
  • Purity
    >89%, by SDS-PAGE with Coomassie Brilliant Blue staining.
  • Activity
    Not tested.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"