Heparin Separopore® 6B

Heparin Separopore® 6B

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SKU
BW-20181210
Catalog Number: BW-20181210
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Application:
Heparin Separopore® 6B is an affinity matrix widely used in affinity purification of various heparin-binding proteins or ligands, such as antithrombin III, lipoprotein, DNA binding proteins (transcription factors, virus coat proteins etc.) and steroid receptors. It can also be used as a high capacity cation exchange medium. Specific proteins can be separated by using different concentrations of salt or a salt gradient. Heparin-Separopore® exhibits excellent binding capacity, a high flow rate, and no significant loss of the heparin ligand. Heparin Separopore® 6B contains heparin (from porcine intestinal mucosa) immobilized by CNBr activation coupling method.

Heparin Separopore exhibits excellent binding capacity, high flow rate, no significant loss of the heparin ligand and a pH stability range of 3-10.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

Technical Specifications:
Ligand: Porcine heparin
Matrix: Separopore® 6B (agarose beads, 6%)
Particle size range: 53 – 180 µm
Molecular weight range: 6 x 104 – 2 x 107
Ligand coupling method: CNBr activation
Ligand density: 5 mg heparin / mL gel
Binding capacity: ~ 2 mg bovine antithrombin / mL gel
pH stability: 3 – 10 (ligand dependent)
Storage: 2 – 8 °C
Supplied as suspension in 20% ethanol containing 0.05 M Sodium Acetate

References:
Heparan sulfate proteoglycans regulate responses to oocyte paracrine signals in ovarian follicle morphogenesis. Endocrinology. (2012) 153: 4544-55.
Interactions of pancreatic cancer and stellate cells are mediated by FGFR1-III isoform expression. Hepatogastroenterology. (2012) 59: 1604-8.
A novel synthetic derivative of human erythropoietin designed to bind to glycosaminoglycans. Drug Deliv. (2012) 19: 202-7.
Pilot production of recombinant human clotting factor IX from transgenic sow milk. J Chromatogr B Analyt Technol Biomed Life Sci. (2012) 898: 78-89.
A novel solid-phase site-specific PEGylation enhances the in vitro and in vivo biostabilty of recombinant human keratinocyte growth factor 1. PLoS One. (2012) 7: e36423.
Solid-phase N-terminus PEGylation of recombinant human fibroblast growth factor 2 on heparin-sepharose column. Bioconjug Chem. (2012) 23: 740-50.
Removing human immunodeficiency virus (HIV) from human blood using immobilized heparin. Biotechnol Lett. (2012) 34: 853-6.
Acceleration of diabetic-wound healing with PEGylated rhaFGF in healing-impaired streptozocin diabetic rats. Wound Repair Regen. (2011) 19: 633-44.
A new recombinant human apolipoprotein E mimetic peptide with high-density lipoprotein binding and function enhancing activity. Exp Biol Med (Maywood). (2011) 236: 1468-76.
TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase. Arch Biochem Biophys. (2011) 516: 75-83.
Purification and characterization of a cytosolic Ca2+-independent phospholipase A(2) from bovine brain. Mol Cells. (2011) 32: 405-13.
Differential effects of murine and human factor X on adenovirus transduction via cell-surface heparan sulfate. J Biol Chem. (2011) 286: 24535-43.
Febuxostat inhibition of endothelial-bound XO: implications for targeting vascular ROS production. Free Radic Biol Med. (2011) 51: 179-84.
Purification and characterization of SepII a new restriction endonuclease from Staphylococcus epidermidis. Microbiol Res. (2012) 167: 90-4.
Characterization of the Mycobacterium avium subsp. Paratuberculosis laminin-binding/histone-like protein (Lbp/Hlp) which reacts with sera from patients with Crohn's disease. Microbes Infect. (2011) 13: 585-94.
Purification and characterization of a second type of neutral ceramidase from rat brain: a second more hydrophobic form of rat brain ceramidase. Biochim Biophys Acta. (2011) 1811: 242-52.
Interaction of phospholipid transfer protein with human tear fluid mucins. J Lipid Res. (2010) 51: 3126-34.
Characterization of a recombinant form of annexin VI for detection of apoptosis. Bioconjug Chem. (2010) 21: 1554-8.
Laminin-121--recombinant expression and interactions with integrins. Matrix Biol. (2010) 29: 484-93.

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Usage: bioWORLD's products are supplied for LABORATORY RESEARCH USE ONLY. The product may not be used as a drug, agricultural or pesticidal product , food additive or as a household chemical.

Hazmat Shipping: Non-hazardous
Storage: 2-8°C
Appearance Form: suspension
Appearance Color: White
Brand Name: bioPLUS™, Separopore®
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