Description
RP1-Heparanase-1 is a polyclonal antibody made to the endo-beta-D-glucuronidase heparanase-1. The antibody is made to a synthetic peptide based on the aminoterminal end of the NTF of human heparanase-1. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Heparanase-1 was discovered as an enzyme in placenta, platelets, sprouting blood vessels and tumors that cleaved the heparin sulfate groups off of the heparan sulfate glycosaminoglycans (HS-GAGs) in the ECM. Since the HS-GAGs act as reservoirs for numerous cationic growth factors and proteinases, the release into the local environment of these factors initiates a wide range of responses. Heparanase-1 is an endo-beta-D-glucuronidase that cleaves glycosidic bonds of heparin sulfate chains by hydrolysis. Heparanase-2 was discovered later, an enzyme with 44% identity to heparanase-1 at the amino acid level. Heparanase-1 is secreted as a zymogen, and the active form is a 2-chain molecule held together by intermolecular disulfide bonds. Two cleavages are required to generate the active form of heparanase-1. The short aminoterminal fragment (NTF) runs from glutamine-36 to glutamic acid-109, and the carboxyterminal fragment (CTF) runs from lysine-158 to isoleucine 543 (the end of the latent molecule). Cleavage at Ala35-Gln36 and Glu109-Ser110 creates the NTF, and cleavage at Gln157-Lys158 generates the CTF. A linker peptide of 72 residues is excised and released to allow the 2-chain molecule to form. The heparin binding site is located at the aminoterminal end of the CTF, and the active residues are Glu225 (the proton donor) and Glu343 (the nucleophile). The enzyme that cleaves the aminoterminus of the CTF is thought to be cathepsin-L, or a related proteinase, since a tyrosine residue sits aminoterminal to the cleavage site at P2. The activation is thought to occur in lysosomal compartments, requiring an acidic pH, and the enzyme is stored there awaiting secretion. The 543 amino acid pro-heparanase-1 sequence predicts a protein of 61.1 kDa, seen as a 65 kDa protein on blots, with a pI of 9.37. The basic pI helps drive to association with HS-GAGs. A 97 amino acid form is also predicted, with a mass of 10.3 kDa and a pI of 5.53. The short form starts at the second methionine, has a deletion starting 23 residues into the NTF, and ends shortly after the nucleophilic glutamic acid. Little is known about the distribution or function of the smaller form. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
Description
RP2-Heparanase-1 is a polyclonal antibody made to the endo-beta-D-glucuronidase heparanase-1. The antibody is made to a synthetic peptide based on the aminoterminal end of the linker fragment of human heparanase-1. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Heparanase-1 was discovered as an enzyme in placenta, platelets, sprouting blood vessels and tumors that cleaved the heparin sulfate groups off of the heparan sulfate glycosaminoglycans (HS-GAGs) in the ECM. Since the HS-GAGs act as reservoirs for numerous cationic growth factors and proteinases, the release into the local environment of these factors initiates a wide range of responses. Heparanase-1 is an endo-beta-D-glucuronidase that cleaves glycosidic bonds of heparin sulfate chains by hydrolysis. Heparanase-2 was discovered later, an enzyme with 44% identity to heparanase-1 at the amino acid level. Heparanase-1 is secreted as a zymogen, and the active form is a 2-chain molecule held together by intermolecular disulfide bonds. Two cleavages are required to generate the active form of heparanase-1. The short aminoterminal fragment (NTF) runs from glutamine-36 to glutamic acid-109, and the carboxyterminal fragment (CTF) runs from lysine-158 to isoleucine 543 (the end of the latent molecule). Cleavage at Ala35-Gln36 and Glu109-Ser110 creates the NTF, and cleavage at Gln157-Lys158 generates the CTF. A linker peptide of 72 residues is excised and released to allow the 2-chain molecule to form. The heparin binding site is located at the aminoterminal end of the CTF, and the active residues are Glu225 (the proton donor) and Glu343 (the nucleophile). The enzyme that cleaves the aminoterminus of the CTF is thought to be cathepsin-L, or a related proteinase, since a tyrosine residue sits aminoterminal to the cleavage site at P2. The activation is thought to occur in lysosomal compartments, requiring an acidic pH, and the enzyme is stored there awaiting secretion. The 543 amino acid pro-heparanase-1 sequence predicts a protein of 61.1 kDa, seen as a 65 kDa protein on blots, with a pI of 9.37. The basic pI helps drive to association with HS-GAGs. A 97 amino acid form is also predicted, with a mass of 10.3 kDa and a pI of 5.53. The short form starts at the second methionine, has a deletion starting 23 residues into the NTF, and ends shortly after the nucleophilic glutamic acid. Little is known about the distribution or function of the smaller form. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
Description
RP3-Heparanase-1 is a polyclonal antibody made to the endo-beta-D-glucuronidase heparanase-1. The antibody is made to a synthetic peptide based on the aminoterminal end of the carboxyterminal fragment of human heparanase-1. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Heparanase-1 was discovered as an enzyme in placenta, platelets, sprouting blood vessels and tumors that cleaved the heparin sulfate groups off of the heparan sulfate glycosaminoglycans (HS-GAGs) in the ECM. Since the HS-GAGs act as reservoirs for numerous cationic growth factors and proteinases, the release into the local environment of these factors initiates a wide range of responses. Heparanase-1 is an endo-beta-D-glucuronidase that cleaves glycosidic bonds of heparin sulfate chains by hydrolysis. Heparanase-2 was discovered later, an enzyme with 44% identity to heparanase-1 at the amino acid level. Heparanase-1 is secreted as a zymogen, and the active form is a 2-chain molecule held together by intermolecular disulfide bonds. Two cleavages are required to generate the active form of heparanase-1. The short aminoterminal fragment (NTF) runs from glutamine-36 to glutamic acid-109, and the carboxyterminal fragment (CTF) runs from lysine-158 to isoleucine 543 (the end of the latent molecule). Cleavage at Ala35-Gln36 and Glu109-Ser110 creates the NTF, and cleavage at Gln157-Lys158 generates the CTF. A linker peptide of 72 residues is excised and released to allow the 2-chain molecule to form. The heparin binding site is located at the aminoterminal end of the CTF, and the active residues are Glu225 (the proton donor) and Glu343 (the nucleophile). The enzyme that cleaves the aminoterminus of the CTF is thought to be cathepsin-L, or a related proteinase, since a tyrosine residue sits aminoterminal to the cleavage site at P2. The activation is thought to occur in lysosomal compartments, requiring an acidic pH, and the enzyme is stored there awaiting secretion. The 543 amino acid pro-heparanase-1 sequence predicts a protein of 61.1 kDa, seen as a 65 kDa protein on blots, with a pI of 9.37. The basic pI helps drive to association with HS-GAGs. A 97 amino acid form is also predicted, with a mass of 10.3 kDa and a pI of 5.53. The short form starts at the second methionine, has a deletion starting 23 residues into the NTF, and ends shortly after the nucleophilic glutamic acid. Little is known about the distribution or function of the smaller form. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
Description
RP4-Heparanase-1 is a polyclonal antibody made to the endo-beta-D-glucuronidase heparanase-1. The antibody is made to a synthetic peptide based on the carboxyterminal end of human heparanase-1. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Heparanase-1 was discovered as an enzyme in placenta, platelets, sprouting blood vessels and tumors that cleaved the heparin sulfate groups off of the heparan sulfate glycosaminoglycans (HS-GAGs) in the ECM. Since the HS-GAGs act as reservoirs for numerous cationic growth factors and proteinases, the release into the local environment of these factors initiates a wide range of responses. Heparanase-1 is an endo-beta-D-glucuronidase that cleaves glycosidic bonds of heparin sulfate chains by hydrolysis. Heparanase-2 was discovered later, an enzyme with 44% identity to heparanase-1 at the amino acid level. Heparanase-1 is secreted as a zymogen, and the active form is a 2-chain molecule held together by intermolecular disulfide bonds. Two cleavages are required to generate the active form of heparanase-1. The short aminoterminal fragment (NTF) runs from glutamine-36 to glutamic acid-109, and the carboxyterminal fragment (CTF) runs from lysine-158 to isoleucine 543 (the end of the latent molecule). Cleavage at Ala35-Gln36 and Glu109-Ser110 creates the NTF, and cleavage at Gln157-Lys158 generates the CTF. A linker peptide of 72 residues is excised and released to allow the 2-chain molecule to form. The heparin binding site is located at the aminoterminal end of the CTF, and the active residues are Glu225 (the proton donor) and Glu343 (the nucleophile). The enzyme that cleaves the aminoterminus of the CTF is thought to be cathepsin-L, or a related proteinase, since a tyrosine residue sits aminoterminal to the cleavage site at P2. The activation is thought to occur in lysosomal compartments, requiring an acidic pH, and the enzyme is stored there awaiting secretion. The 543 amino acid pro-heparanase-1 sequence predicts a protein of 61.1 kDa, seen as a 65 kDa protein on blots, with a pI of 9.37. The basic pI helps drive to association with HS-GAGs. A 97 amino acid form is also predicted, with a mass of 10.3 kDa and a pI of 5.53. The short form starts at the second methionine, has a deletion starting 23 residues into the NTF, and ends shortly after the nucleophilic glutamic acid. Little is known about the distribution or function of the smaller form. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 at -20C.
