Product: HPSE Antibody
Catalog: DF12411
Description: Rabbit polyclonal antibody to HPSE
Application: WB IHC
Reactivity: Human, Mouse
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
Mol.Wt.: 60 kDa; 61kD(Calculated).
Uniprot: Q9Y251
RRID: AB_2845216

View similar products>>

   Size Price Inventory
 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse
Prediction:
Pig(92%), Zebrafish(100%), Bovine(83%), Horse(100%), Sheep(92%), Rabbit(100%), Dog(100%), Chicken(83%)
Clonality:
Polyclonal
Specificity:
HPSE Antibody detects endogenous levels of total HPSE.
RRID:
AB_2845216
Cite Format: Affinity Biosciences Cat# DF12411, RRID:AB_2845216.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Endo glucoronidase; Endo-glucoronidase; HEP; Heparanase 50 kDa subunit; Heparanase; Heparanase-1; Heparanase1; Hpa 1; HPA; Hpa1; HPR 1; HPR1; HPSE 1; HPSE; HPSE_HUMAN; HPSE1; HSE 1; HSE1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
Q9Y251 HPSE_HUMAN:

Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase.

Sequence:
MLLRSKPALPPPLMLLLLGPLGPLSPGALPRPAQAQDVVDLDFFTQEPLHLVSPSFLSVTIDANLATDPRFLILLGSPKLRTLARGLSPAYLRFGGTKTDFLIFDPKKESTFEERSYWQSQVNQDICKYGSIPPDVEEKLRLEWPYQEQLLLREHYQKKFKNSTYSRSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLLLDYCSSKGYNISWELGNEPNSFLKKADIFINGSQLGEDFIQLHKLLRKSTFKNAKLYGPDVGQPRRKTAKMLKSFLKAGGEVIDSVTWHHYYLNGRTATKEDFLNPDVLDIFISSVQKVFQVVESTRPGKKVWLGETSSAYGGGAPLLSDTFAAGFMWLDKLGLSARMGIEVVMRQVFFGAGNYHLVDENFDPLPDYWLSLLFKKLVGTKVLMASVQGSKRRKLRVYLHCTNTDNPRYKEGDLTLYAINLHNVTKYLRLPYPFSNKQVDKYLLRPLGPHGLLSKSVQLNGLTLKMVDDQTLPPLMEKPLRPGSSLGLPAFSYSFFVIRNAKVAACI

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Horse
100
Dog
100
Zebrafish
100
Rabbit
100
Pig
92
Sheep
92
Bovine
83
Chicken
83
Xenopus
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - Q9Y251 As Substrate

Site PTM Type Enzyme
K98 Acetylation
T99 Phosphorylation
Y156 Phosphorylation
N162 N-Glycosylation
Y165 Phosphorylation
N178 N-Glycosylation
N200 N-Glycosylation
N217 N-Glycosylation
N238 N-Glycosylation
K262 Ubiquitination
S332 Phosphorylation
T333 Phosphorylation
Y348 Phosphorylation
K427 Acetylation
N459 N-Glycosylation
T507 Phosphorylation

Research Backgrounds

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.

PTMs:

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.

Subcellular Location:

Lysosome membrane>Peripheral membrane protein. Secreted. Nucleus.
Note: 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).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase.

Subunit Structure:

Heterodimer; heterodimer formation between the 8 kDa and the 50 kDa subunits is required for enzyme activity. Interacts with TF; the interaction, inhibited by heparin, enhances the generation of activated factor X and activates coagulation. Interacts with HRG; the interaction is enhanced at acidic pH, partially inhibits binding of HPSE to cell surface receptors and modulates its enzymatic activity. Interacts with SDC1; the interaction enhances the shedding of SDC1. Interacts with HPSE2.

Family&Domains:

Belongs to the glycosyl hydrolase 79 family.

Research Fields

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Metabolism > Glycan biosynthesis and metabolism > Glycosaminoglycan degradation.

· Metabolism > Global and overview maps > Metabolic pathways.

References

1). Piperazine ferulate prevents high‑glucose‑induced filtration barrier injury of glomerular endothelial cells. Experimental and Therapeutic Medicine (PubMed: 34504620) [IF=2.7]

Application: WB    Species: Human    Sample: glomerular endothelial cells (GEnCs)

Figure 2 AMPK regulates the expression of Hpa-1 and TJ proteins. (A) Western blot analysis of Hpa-1, Sdc-1, occludin-1 and ZO-1 expression. Densitometric analysis of (B) Hpa-1 and (C) Sdc-1 expression. (D) Expression levels of Sdc-1 in the cell culture supernatant. (E) Densitometric analysis of occludin-1 and (F) ZO-1 expression. Data are presented as the mean ± standard deviation of three repeats. *P<0.05, **P<0.01, ***P<0.001 vs. the control group; #P<0.05, ##P<0.01 vs. HG. AMPK, adenosine monophosphate-activated protein kinase; Hpa-1, heparanase-1; TJ, tight junction; Sdc-1, syndecan-1; ZO-1, Zonula occludens-1; HG, high glucose.

Application: IHC    Species: Human    Sample: glomerular endothelial cells (GEnCs)

Figure 5 PF alleviates endothelial glycocalyx injury in vivo. (A) Transmission electron microscopy of glomeruli extracted from different groups of animals. (B) The number of glomerular endothelial fenestrations. (C) FITC-WGA staining for endothelial glycocalyx in the glomerulus. Magnification, x400. (D) Quantification analysis of FITC-WGA staining. (E) Immunohistochemical images of p-AMPKα (Thr-172). Magnification, x400. (F) Quantification analysis of immunohistochemical staining of p-AMPKα (Thr-172). (G) Immunohistochemical staining of Hpa-1. Magnification, x400. (H) Quantification analysis of immunohistochemical staining of Hpa-1. Data are presented as the mean ± standard deviation of three repeats. **P<0.01, ***P<0.01 vs. the control group; #P<0.05, ##P<0.01 vs. the model group. PF, piperazine ferulate; FITC, fluorescein isothiocyanate; WGA, wheat germ agglutinin; p-, phosphorylated-; AMPK, adenosine monophosphate-activated protein kinase; Hpa-1, heparanase-1.

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.