"NMR"

Supplier: SP Industries

PTFE/silicone rubber septum for 4 and 5 mm tubes

Supplier: LGC Standards PROMOCHEM

The purity estimate by traditional analytical techniques was obtained by subtraction from 100% of total impurities by HPLC with UV detection, Karl Fischer analysis, thermogravimetric analysis and 1H NMR is 99,3 ± 1,3% mass fraction, (95% coverage interval). Supporting evidence is provided by elemental microanalysis.

Supplier: LGC Standards PROMOCHEM

Purity estimate obtained by subtraction from 100% of total impurities by GC-FID, thermogravimetric analysis, Karl Fischer analysis and 1H NMR is 99,1 ± 1,4% mass fraction, (95% coverage interval). Supporting evidence is provided by elemental microanalysis.

Supplier: SP Industries

Glass, class A. These long-tip sample transfer pipettes are ideal for the easy addition or removal of liquid samples from the longest NMR and EPR sample tubes, volumetric flasks with long, narrow necks and chromatography columns.

Supplier: LGC Standards PROMOCHEM

The purity value obtained from a combination of traditional analytical techniques is 99,6 ± 1,4% mass fraction, (95% coverage interval). The purity estimate by traditional analytical techniques was obtained by subtraction from 100% of total impurities by GC-FID, thermogravimetric analysis, Karl Fischer analysis and 1H NMR and also supported by elemental microanalysis.

Supplier: Merck

1,5,7-Triazabicyclo[4.4.0]dec-5-ene, a bicyclic guanidine base, is an excellent catalyst for Michael and Michael-type reactions. It forms 1:1 complex with lasalocid acid and crystal structure of the complex has been studied by X-ray diffraction, FT-IR spectroscopy and H NMR.

Supplier: KLEINFELD

This washer is used for rapid, safe washing and drying of cuvettes, tubes and small scale volumetric items up to approximately 22 mm OD.

Supplier: Merck

Lithium bis(trifluoromethylsulphonyl)imide, Sigma-Aldrich®

Supplier: HAMILTON BONADUZ

Electrodes for special laboratory applications such as microbiological samples, serum, flat surfaces, small volumes, and samples containing fats and proteins.

Supplier: SI Analytics

For small sample volumes in life science and pharmaceutical applications.

Supplier: biotechrabbit

Accessories and supplements for Rapid Translation System (RTS).

Supplier: Enzo Life Sciences

The multifunctional, multi -compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins, as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the solub le paralog of the ER membrane protein Calnexin (Cnx). Crt's three domains include a 180 residue N-terminal domain, a proline-rich Pdomainresidues 189 -288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P -domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N -glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Supplier: Enzo Life Sciences

The multifunctional, multi -compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins, as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the solub le paralog of the ER membrane protein Calnexin (Cnx). Crt's three domains include a 180 residue N-terminal domain, a proline-rich Pdomainresidues 189 -288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P -domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N -glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Supplier: Enzo Life Sciences

The multifunctional, multi-compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the soluble paralog of the ER membrane protein Calnexin (Cnx). Crts three domains include a 180 residue N-terminal domain, a proline-rich P-domain (residues 189-288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P-domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N-glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Supplier: SP Industries

Sapphire NMR Tubes 1 * 1 items

Supplier: SP Industries

NMR TUBE SAMPLE 5MM 1 * 1 items