Recombinant Human Heparanase 1 protein (denatured) is a Human Full Length protein, in the 36 to 543 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
Amino acid sequence
M G S S H H H H H H S S G L V P R G S H M G S Q D V V D L D F F T Q E P L H L V S P S F L S V T I D A N L A T D P R F L I L L G S P K L R T L A R G L S P A Y L R F G G T K T D F L I F D P K K E S T F E E R S Y W Q S Q V N Q D I C K Y G S I P P D V E E K L R L E W P Y Q E Q L L L R E H Y Q K K F K N S T Y S R S S V D V L Y T F A N C S G L D L I F G L N A L L R T A D L Q W N S S N A Q L L L D Y C S S K G Y N I S W E L G N E P N S F L K K A D I F I N G S Q L G E D F I Q L H K L L R K S T F K N A K L Y G P D V G Q P R R K T A K M L K S F L K A G G E V I D S V T W H H Y Y L N G R T A T K E D F L N P D V L D I F I S S V Q K V F Q V V E S T R P G K K V W L G E T S S A Y G G G A P L L S D T F A A G F M W L D K L G L S A R M G I E V V M R Q V F F G A G N Y H L V D E N F D P L P D Y W L S L L F K K L V G T K V L M A S V Q G S K R R K L R V Y L H C T N T D N P R Y K E G D L T L Y A I N L H N V T K Y L R L P Y P F S N K Q V D K Y L L R P L G P H G L L S K S V Q L N G L T L K M V D D Q T L P P L M E K P L R P G S S L G L P A F S Y S F F V I R N A K V A A C I
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Target data
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 a 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.
Alternative names
HEP, HPA, HPA1, HPR1, HPSE1, HSE1, HPSE, Heparanase, Endo-glucoronidase, Heparanase-1, Hpa1
Recommended products
Recombinant Human Heparanase 1 protein (denatured) is a Human Full Length protein, in the 36 to 543 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
Key facts
- Purity
- >85% SDS-PAGE
- Expression system
- Escherichia coli
- Tags
- His tag N-Terminus
- Applications
- SDS-PAGE
- Biologically active
- No
- Accession
- Q9Y251-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 2.4% Urea, 0.32% Tris HCl
Sequence info
Amino acid sequence
- M G S S H H H H H H S S G L V P R G S H M G S Q D V V D L D F F T Q E P L H L V S P S F L S V T I D A N L A T D P R F L I L L G S P K L R T L A R G L S P A Y L R F G G T K T D F L I F D P K K E S T F E E R S Y W Q S Q V N Q D I C K Y G S I P P D V E E K L R L E W P Y Q E Q L L L R E H Y Q K K F K N S T Y S R S S V D V L Y T F A N C S G L D L I F G L N A L L R T A D L Q W N S S N A Q L L L D Y C S S K G Y N I S W E L G N E P N S F L K K A D I F I N G S Q L G E D F I Q L H K L L R K S T F K N A K L Y G P D V G Q P R R K T A K M L K S F L K A G G E V I D S V T W H H Y Y L N G R T A T K E D F L N P D V L D I F I S S V Q K V F Q V V E S T R P G K K V W L G E T S S A Y G G G A P L L S D T F A A G F M W L D K L G L S A R M G I E V V M R Q V F F G A G N Y H L V D E N F D P L P D Y W L S L L F K K L V G T K V L M A S V Q G S K R R K L R V Y L H C T N T D N P R Y K E G D L T L Y A I N L H N V T K Y L R L P Y P F S N K Q V D K Y L L R P L G P H G L L S K S V Q L N G L T L K M V D D Q T L P P L M E K P L R P G S S L G L P A F S Y S F F V I R N A K V A A C I
- Accession
- Q9Y251
- Protein length
- Full Length
- Predicted molecular weight
- 60 kDa
- Amino acids
- 36 to 543
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
General info
- 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 a 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.
- Sequence similarities
Belongs to the glycosyl hydrolase 79 family.
- Post-translational modifications
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.
- Subcellular localisation
- Lysosome membrane, Nucleus
Storage
- Shipped at conditions
- Blue Ice
- Appropriate short-term storage duration
- 1-2 weeks
- Appropriate short-term storage conditions
- +4°C
- Appropriate long-term storage conditions
- -20°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
Heparanase 1 also known as HPA1 or HPSE is an endo-β-D-glucuronidase enzyme with a molecular mass of approximately 50 kDa. It functions mechanically by cleaving heparan sulfate (HS) chains which are long sugar chains found on the extracellular matrix and cell surfaces. This cleavage activity remodels the matrix and influences cell behavior. Heparanase 1 is mainly expressed in the placenta lymphoid tissues and various tumor cells where it plays a role in matrix degradation and cell migration.
- Biological function summary
When heparan sulfate is cleaved by Heparanase 1 it causes the release of HS-bound growth factors and cytokines making them available to cells. This enzymatic activity facilitates cell proliferation and angiogenesis affecting processes important for tissue repair and cancer progression. Heparanase 1 does not require a complex for its function but operates as a monomeric enzyme. Its activity is investigated using assays like heparanase activity assays or ELISA for measuring the enzyme's activity in different biological contexts including mouse models.
- Pathways
The activity of Heparanase 1 intersects significantly with the regulation of angiogenesis and cell signaling pathways such as the VEGF and FGF pathways. These pathways are important for new blood vessel formation making them significant in both normal development and cancer. Heparanase 1 interacts with proteins such as VEGF which is important for blood vessel growth and integrins which are involved in cell-matrix interactions and signaling.
- Associated diseases and disorders
Heparanase 1 is associated with tumor metastasis and inflammation. Its ability to degrade the extracellular matrix enables cancer cell invasion and metastasis. The enzyme also plays a role in inflammatory diseases where it modulates the immune response. Through these disease pathways it relates to other proteins such as matrix metalloproteinases (MMPs) which also participate in matrix remodeling during tumor progression and inflammation.
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1 product image
SDS-PAGE - Recombinant Human Heparanase 1 protein (denatured) (ab181927)
15% SDS-PAGE analysis of ab181927 (3μg)
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