Product nameRecombinant Human Heparan Sulfate Proteoglycan 2/Perlecan protein (Tagged)
Protein lengthProtein fragment
Amino Acid Sequence
SequenceGLRAYDGLSLPEDIETVTASQMRWTHSYLSDDEDMLADSISGDDLGSGDL GSGDFQMVYFRALVNFTRSIEYSPQLEDAGSREFREVSEAVVDTLESEYL KIPGDQVVSV
Molecular weight38 kDa including tags
Amino acids25 to 134
TagsGST tag N-Terminus
Our Abpromise guarantee covers the use of ab114285 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Protein concentration is above or equal to 0.05 µg/µl
Best use within three months from the date of receipt of this protein.
This product was previously labelled as Heparan Sulfate Proteoglycan 2
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.3% Glutathione, 0.79% Tris HCl
- Basement membrane specific heparan sulfate proteoglycan core protein
- Endorepellin (domain V region)
- Heparan sulfate proteoglycan of basement membrane
FunctionIntegral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development.
Endorepellin in an anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.
The LG3 peptide has anti-angiogenic properties that require binding of calcium ions for full activity.
Tissue specificityFound in the basement membranes.
Involvement in diseaseDefects in HSPG2 are the cause of Schwartz-Jampel syndrome (SJS1) [MIM:255800]; a rare autosomal recessive disorder characterized by permanent myotonia (prolonged failure of muscle relaxation) and skeletal dysplasia, resulting in reduced stature, kyphoscoliosis, bowing of the diaphyses and irregular epiphyses.
Defects in HSPG2 are the cause of dyssegmental dysplasia Silverman-Handmaker type (DDSH) [MIM:224410]. The dyssegmental dysplasias are rare, autosomal recessive skeletal dysplasias with anisospondyly and micromelia. There are two recognized types: the severe, lethal DDSH and the milder Rolland-Desbuquois form. Individuals with DDSH also have a flat face, micrognathia, cleft palate and reduced joint mobility, and frequently have an encephalocoele. The endochondral growth plate is short, the calcospherites (which are spherical calcium-phosphorus crystals produced by hypertrophic chondrocytes) are unfused, and there is mucoid degeneration of the resting cartilage.
Sequence similaritiesContains 4 EGF-like domains.
Contains 22 Ig-like C2-type (immunoglobulin-like) domains.
Contains 11 laminin EGF-like domains.
Contains 3 laminin G-like domains.
Contains 3 laminin IV type A domains.
Contains 4 LDL-receptor class A domains.
Contains 1 SEA domain.
modificationsProteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide.
N- and O-glycosylated; contains three heparan sulfate chains. The LG3 peptide contains at least three and up to five potential O-glycosylation sites but no N-glycosylation.
Cellular localizationSecreted > extracellular space > extracellular matrix > basement membrane.
- Information by UniProt
ab114285 has not yet been referenced specifically in any publications.