Heparin - CAS 9005-49-6
Catalog number: 9005-49-6
Category: Inhibitor
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Molecular Weight:
Heparin, a highly sulfated glycosaminoglycan, is widely used as an injectable anticoagulant, and has the highest negative charge density of any known biological molecule. The common form is the sodium salt form.
Heparin; Adomiparin; Bemiparin; Certoparin; Dalteparin; Eparina; Fraxiparin; M118; M-118; M 118; Nadroparine; Parvoparin; Thromboliquine;
Canonical SMILES:
1.Heparin functionalisation of porous PLGA scaffolds for controlled, biologically relevant delivery of growth factors for soft tissue engineering
Geraldine Rohman, Simon C. Baker, Jennifer Southgate and Neil R. Cameron*. J. Mater. Chem., 2009, 19, 9265–9273
The introduction of amino-PEG moieties into PLGA scaffolds not only improved the poor hydrophilicity of the polymeric matrix (visual inspection of wettability), but also provided the necessary active sites for the further grafting of heparin. Heparin was grafted onto scaffolds by the process represented in Fig. 2. Heparin solution loaded over aminated PLGA scaffolds was allowed to react with EDAC as a coupling agent. Different concentrations of heparin solution were loaded over PLGA scaffolds and the process was also carried out with non-aminated control scaffolds to assess heparin adsorption (Table 1). For control scaffolds, the amount of adsorbed heparin was small for heparin loading solution concentrations ≤2.5 mg mL-1 and then the amount increased to 2.1 ± 0.4 mg mg-1 scaffold with a heparin loading solution concentration of 10 mg mL-1. The near absence of colour in foams after the toluidine blue assay showed that the non-covalently immobilised heparin was released completely from non-aminated scaffolds.
2.Bio-functionalization of ligand-free upconverting lanthanide doped nanoparticles for bio-imaging and cell targeting
Nicoleta Bogdan, John A. Capobianco*. Nanoscale, 2012, 4, 3647
The presence of heparin on the Ln3+-UCNPs enables functionalization with bFGF and at the same time maintains dispersibility in an aqueous medium. More importantly, the interaction of bFGF with heparin results in the required conformation of bFGF to interact with the bFGF receptors on the cell membrane.24 FTIR spectroscopy was used to show the successful binding of bFGF to the surface of the heparin coated nanoparticles. This was confirmed by the change in the peaks associated with the S=O stretching, that can be attributed to the interaction between the heparin and bFGF (Fig. 2). This observation agrees with previous studies where the importance of the 2-O- and N-sulfate groups of heparin for the interaction with the amino acid residues in heparin-binding regions of bFGF has been demonstrated. The zeta potential of the bFGF–heparin functionalized UCNPs was measured and a value of 6 mV was obtained. The concentration of bFGF bound on the surface of the heparin-capped Ln3+-UCNPs was obtained using the Bradford assay.
3.Mimicking the receptor-aided binding of HIV-1 TAT protein transduction domains to phospholipid monolayers at the air–water interface
Daehyun Hong, Kwanwoo Shin,* Michael James and Giyoong Tae. Soft Matter, 2012, 8, 8616–8623
Many growth factors and various ECM proteins have strong affinities to heparin via heparin-binding domains, and thus some of the main functions of heparin/heparan sulfate are to facilitate interactions between cells and growth factors or ECM proteins, and to preserve and prolong the effect of growth factors by sequestering them.15 Also, heparin and heparan sulfate have been considered as key GAG molecules that promote intracellular transport of transcription-activating factor (TAT), TAT-derived peptide (TAT-TDP) molecules and arginine-rich peptides. Heparin added to a medium has been reported to compete with these peptides for binding to the cell surface, thus inhibiting their intracellular transport. In addition, a deficiency in the expression of heparan sulfate on the cell surface significantly lowers the number of peptide molecules taken up by the cells.
4.Application of the ‘gate effect’ of a molecularly imprinted polymer grafted on an electrode for the real-time sensing of heparin in blood
Yasuo Yoshimi,* Kuniaki Sato, Masaki Ohshima and Elena Piletska. Analyst, 2013, 138, 5121–5128
The cyclic voltammogram of potassium ferrocyanide on the surface of the MIP–ITO or NIP–ITO electrode in the presence and absence of heparin is shown in Fig. 1. The current density of ferrocyanide at the MIP–ITO electrode was significantly smaller than that at the NIP–ITO or untreated ITO electrode: the peak current densities in the absence of heparin were 0.91± 0.08, 1.38±0.04 and 1.48±0.02 mA cm2, respectively, n = 3 each. The peak potentials were very similar among the electrodes (0.32–0.33 V versus Ag/AgCl). 0.04 units per mL of heparin increased the current at the MIP–ITO surface, while 40 units per mL of heparin decreased the current. The peak potential did not change in the presence of heparin. The current density at the NIP–ITO electrode was also not dependent on the presence of heparin.
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CAS 9005-49-6 Heparin

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