Recombinant Rat Heparanase (HPSE) Protein (His&Myc)

Name: Recombinant Rat Heparanase (HPSE) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-04948P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Rat Heparanase (HPSE) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q71RP1
Target Symbol	HPSE
Synonyms	Hpse; HepHeparanase; EC 3.2.1.166; Endo-glucoronidase) [Cleaved into: Heparanase 8 kDa subunit; Heparanase 50 kDa subunit]
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	KDVVDLEFYTKRLFQSVSPSFLSITIDASLATDPRFLTFLGSPRLRALARGLSPAYLRFGGTKTDFLIFDPNKE
Expression Range	29-102aa
Protein Length	Partial
Mol. Weight	15.8 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Subcellular Location	Lysosome membrane; Peripheral membrane protein. Secreted. Nucleus.
Protein Families	Glycosyl hydrolase 79 family
Database References	KEGG: rno:64537 UniGene: PMID: 28720149 Endothelial cell-to-cardiomyocyte transfer of heparanase to modulates the cardiomyocyte cell death signature. This mechanism was observed in the acutely diabetic heart, and its interruption following chronic diabetes may contribute towards the development of diabetic cardiomyopathy. PMID: 27979811 the expression of the gene for heparanase was increased in the right and left ventricles after treatment with monocrotaline PMID: 26638897 Inhibiting heparanase function could offer a new strategy for managing cardiomyopathy observed after diabetes. PMID: 24608441 Suggest that the heparanase-lipoprotein lipase-VEGF axis amplifies fatty acid delivery, a rapid and adaptive mechanism that is geared to overcome the loss of glucose consumption by the diabetic heart. PMID: 24115032 active heparanase released lipoprotein lipase from the myocyte surface PMID: 23471235 Heparanase and TFPI are locally elevated in the process of avascular necrosis and are normalized on treatment. PMID: 23063054 Heparanase gene is involved in heparan sulfate proteoglycans metabolism. PMID: 22339633 HPR1 production is increased in endothelial cells from rat models of diabetes, and in macrophages in atherosclerotic lesions of diabetic and nondiabetic patients. Increased HPR1 production may contribute to pathogenesis and progression of atherosclerosis. PMID: 21424539 Heparanase was upregulated and associated with increased VEGF in streptozotocin diabetic rat retinas. Heparanase may be involved in development of diabetic retinopathy and may be possible novel target for therapeutic intervention. PMID: 20130710 Characterization of a novel intracellular heparanase that has a FERM domain. PMID: 11988100 characterization of rat heparanase activity in a parathyroid cell line PMID: 12077130 heparanase gene transcription is regulated in activated T cells by early growth response 1 PMID: 14522979 Heparanase plays a role in ovaian tissue remodeling during folliculogenesis and forpus luteum formation and regression. PMID: 15728796 heparanase contributes to the pathogenesis of proteinuria in a model of anti-GBM disease PMID: 15877677 Results describe the cellular localization of heparanase and its colocalization with syndecan-3 in spinal cords of adult rats. PMID: 16320243 These results suggest involvement of radicals and angiotensin II in the modulation of glomerular basement membrane permeability through heparan sulfate and heparanase expression. PMID: 16899518 HPSE is involved in the pathogenesis of proteinuria in overt diabetic nephropathy by degradation of heparan sulfates PMID: 17051139 The expression of heparanase by astrocytes may correlate with the time of migration of reactive astrocytes toward the ischemic core, resulting in astrogliosis. This suggests a novel role of heparanase in the pathophysiology of brain ischemia. PMID: 17368723 Results suggest the involvement of heparanase in the migration or invasion of microglia or brain macrophages across basement membrane around brain vasculature. PMID: 18222122 results suggest heparanase expression increases after castration & correlates with decreased heparan sulfate; variation in heparanase expression is involved in tissue remodeling & control of regressive pattern after 1 week of androgen deprivation PMID: 18278514 role for heparanase in the regulation of arterial structure, mechanics, and repair PMID: 19096032 Following hyperglycemia, translocation of lipoprotein lipase from cardiomyocytes to endothelial cells is dependent on fatty acids to increase endothelial intracellular heparanase followed by secretion of heparanase by glucose. PMID: 19218500

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.