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Mouse Anti-HPSE Recombinant Antibody (A261) (CBMAB-AP2952LY)

The product is antibody recognizes HPSE. The antibody A261 immunoassay techniques such as: ICC, IHC, IP, WB.
See all HPSE antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
A261
Antibody Isotype
IgG2a, λ
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Recombinant Heparanase (HPA)
Specificity
Human
Antibody Isotype
IgG2a, λ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
Affinity purity
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Heparanase
Introduction
Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. The protein encoded by this gene is an enzyme that cleaves heparan sulfate proteoglycans to permit cell movement through remodeling of the extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2011]
Entrez Gene ID
10855
UniProt ID
Q9Y251
Alternative Names
Heparanase; Endo-Glucoronidase; Heparanase-1; HPSE1; HPA1; HPR1;
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.
Biological Process
Angiogenesis involved in wound healing Source: GO_Central
Cell-matrix adhesion Source: UniProtKB
Establishment of endothelial barrier Source: Ensembl
Factor XII activation Source: ComplexPortal
Heparan sulfate proteoglycan catabolic process Source: ComplexPortal
Heparin metabolic process Source: Ensembl
Inflammatory response Source: ComplexPortal
Positive regulation of angiogenesis Source: ComplexPortal
Positive regulation of autophagy Source: ComplexPortal
Positive regulation of blood coagulation Source: ComplexPortal
Positive regulation of cell-matrix adhesion Source: ComplexPortal
Positive regulation of cell migration Source: ComplexPortal
Positive regulation of cell population proliferation Source: ComplexPortal
Positive regulation of hair follicle development Source: Ensembl
Positive regulation of osteoblast proliferation Source: UniProtKB
Positive regulation of protein kinase B signaling Source: UniProtKB
Positive regulation of substrate adhesion-dependent cell spreading Source: ComplexPortal
Positive regulation of vascular endothelial growth factor production Source: UniProtKB
Protein transmembrane transport Source: Ensembl
Proteoglycan metabolic process Source: ProtInc
Regulation of hair follicle development Source: UniProtKB
Response to organic substance Source: Ensembl
Vascular wound healing Source: Ensembl
Cellular Location
Nucleus; Secreted; Lysosome membrane. Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity).
PTM
Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme.
N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.

Yang, Y., Yuan, F., Zhou, H., Quan, J., Liu, C., Wang, Y., ... & Yu, X. (2023). Potential roles of heparanase in cancer therapy: Current trends and future direction. Journal of Cellular Physiology, 238(5), 896-917.

de Boer, C., Armstrong, Z., Lit, V. A., Barash, U., Ruijgrok, G., Boyango, I., ... & Wu, L. (2022). Mechanism-based heparanase inhibitors reduce cancer metastasis in vivo. Proceedings of the National Academy of Sciences, 119(31), e2203167119.

Gallard, C., Lebsir, N., Khursheed, H., Reungoat, E., Plissonnier, M. L., Bré, J., ... & Grigorov, B. (2022). Heparanase-1 is upregulated by hepatitis C virus and favors its replication. Journal of Hepatology, 77(1), 29-41.

Yang, W. J., Shi, L., Wang, X. M., & Yang, G. W. (2021). Heparanase is a novel biomarker for immune infiltration and prognosis in breast cancer. Aging (Albany NY), 13(16), 20836.

Koganti, R., Suryawanshi, R., & Shukla, D. (2020). Heparanase, cell signaling, and viral infections. Cellular and Molecular Life Sciences, 77, 5059-5077.

Agelidis, A., & Shukla, D. (2020). Heparanase, heparan sulfate and viral infection. Heparanase: From Basic Research to Clinical Applications, 759-770.

Buijsers, B., Yanginlar, C., de Nooijer, A., Grondman, I., Maciej-Hulme, M. L., Jonkman, I., ... & van der Vlag, J. (2020). Increased plasma heparanase activity in COVID-19 patients. Frontiers in immunology, 11, 575047.

Theodoro, T. R., Matos, L. L., Cavalheiro, R. P., Justo, G. Z., Nader, H. B., & Pinhal, M. A. S. (2019). Crosstalk between tumor cells and lymphocytes modulates heparanase expression. Journal of Translational Medicine, 17(1), 1-14.

Wei, R. R., Sun, D. N., Yang, H., Yan, J., Zhang, X., Zheng, X. L., ... & Ding, J. (2018). CTC clusters induced by heparanase enhance breast cancer metastasis. Acta Pharmacologica Sinica, 39(8), 1326-1337.

Lv, Q., Wu, K., Liu, F., Wu, W., Chen, Y., & Zhang, W. (2018). Interleukin‑17A and heparanase promote angiogenesis and cell proliferation and invasion in cervical cancer. International Journal of Oncology, 53(4), 1809-1817.

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For research use only. Not intended for any clinical use.

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