Analytical Data
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Gene name
HPSE
- Application
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Alternative Names
HPSE;HEP;HPA;HPA1;Heparanase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y251
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Expression Region
36-543aa
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AA Sequence
QDVVDLDFFTQEPLHLVSPSFLSVTIDANLATDPRFLILLGSPKLRTLAR GLSPAYLRFGGTKTDFLIFDPKKESTFEERSYWQSQVNQDICKYGSIPPD VEEKLRLEWPYQEQLLLREHYQKKFKNSTYSRSSVDVLYTFANCSGLDLI FGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNEPNSFLKKADI FINGSQLGEDFIQLHKLLRKSTFKNAKLYGPDVGQPRRKTAKMLKSFLKA GGEVIDSVTWHHYYLNGRTATKEDFLNPDVLDIFISSVQKVFQVVESTRP GKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSARMGIEVVMRQVF FGAGNYHLVDENFDPLPDYWLSLLFKKLVGTKVLMASVQGSKRRKLRVYL HCTNTDNPRYKEGDLTLYAINLHNVTKYLRLPYPFSNKQVDKYLLRPLGP HGLLSKSVQLNGLTLKMVDDQTLPPLMEKPLRPGSSLGLPAFSYSFFVIR NAKVAACI
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Molecular Weight
78 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
Related Products
Identification
Protein Description
HPSE (Heparanase) is an endo-β-glucuronidase enzyme that plays a significant role in the degradation of heparan sulfate, a key component of the extracellular matrix. The research on HPSE has gained momentum due to its pivotal involvement in various physiological and pathological processes, including tumor metastasis, inflammation, and angiogenesis. Elevated HPSE activity has been linked to several malignancies, making it a potential target for therapeutic intervention. Recent studies have focused on elucidating the structural and functional characteristics of HPSE, particularly in its recombinant form, to understand its enzymatic mechanisms and interactions with heparan sulfate. The recombinant protein serves as a valuable tool for investigating HPSE's role in disease progression and for developing HPSE inhibitors that could inhibit its enzymatic activity, thereby opening new avenues for cancer treatment and other related disorders. The exploration of HPSE not only enhances our understanding of tumor biology but also paves the way for innovative therapeutic strategies aimed at modulating its activity for clinical benefit.
