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Showing 1-30 of 177 results for "88-72-2"
The Effective Use of Protein Kinase Inhibitors
-K1b 16 72 37 79 89 88 86 93 83 95 92 70 20 95 95 78 2 9 2 MAPKAP-K2 99 99 90 5 59 102 98 95 93 97 102 74 90 125 72 98 103 90...
The Effective Use of Protein Kinase Inhibitors
-K1b 16 72 37 79 89 88 86 93 83 95 92 70 20 95 95 78 2 9 2 MAPKAP-K2 99 99 90 5 59 102 98 95 93 97 102 74 90 125 72 98 103 90...
Product Information Sheet - 80476
of 5 Figure 2: Product Drawing DUO +34 deg C Run-Time acceleration with temp 70 ...
Product Information Sheet - 92451
Temperature* Run-Out Window** Time Marks in Hours +25°C/+77°F +22°C/+72°F 12 hours 0.5, 1, 2, 4, 8, 12 * The temperature at which the run-time advancement...
Product Information Sheet - L6882
Fluids. Methods in Enzymology, 57, 65- 72 (1978). 5. Karl, D. M., Determination of GTP, GDP, and GMP in Cell and Tissue Extracts. Methods in Enzymology, 57, 88 (1978). ALF/RXR 9/02 Sigma brand
Data Sheet - SRP5208
43 72 95 130 170 56 34 References 1. Speck, O. et al., Moesin functions antagonistically to the Rho pathway to maintain epithelial integrity. Nature, 421(6918), 83-7 (2003). 2. Lankes
Product Information Sheet - 11636103001
��������œ�"(3�"!/ /!E� H,/!S!/E2(� R�$�"4!�\g!N"�8� �88!72!$%!9D!E�!%"!DH!E�Q%$��!C%�73� 9D!E�!%"!DH!E� ��������� ������� ����� ������
Product Information Sheet - P4020
and Polycations on the Classical and Alternative Pathways of Complement. Immunopharmacology, 17(2), 65-72 (1989). 6. Martindale The Extra Pharmacopoeia, 30th ed., Reynolds, J.E.F., ed., The Pharmaceutical
Product Information Sheet - O8801
90836e (1977). 29• N.S. Zabel'nikov, O.A. Agapov, and V.D. Vorob'ev, Plast. Massy, 72 (1977); Chem. Abstr., 88, 51411 (1978). 30• F.P. Darmory and M. Dibenedetto, U.S. Patent 4,016,173 (1977); Chem
Product Information Sheet - C5896
activity remaining after 16 hours. References 1. Ohta-Fukuyama, M. et al., J. Biochem., 88(1), 197- 203 (1980). 2. Allouche-Arnon, H. et al., Chem. Commun., 49, 7076-7078 (2013). 3. Takayama, M.
Data Sheet - G1166
(1996). 9. Karlsen, A.E., et al., Proc. Natl. Acad. Sci., 88, 8337 (1991). 10. Michelsen, B.K., et al., Proc. Natl. Acad. Sci., 88, 8754 (1991). 11. Kaufman, D.L. et al., J. Neurochem., 56
Product Information Sheet - L9504
Fluids. Methods in Enzymology, 57, 65- 72 (1978). 5. Karl, D.M., Determination of GTP, GDP, and GMP in Cell and Tissue Extracts. Methods in Enzymology, 57, 88 (1978). IRB/RXR 10/07 Sigma
Product Information Sheet - M2537
in DMSO at 25 mg/mL. Storage/Stability Store the powder at 2-8°C. References 1. Endo, A. et al., FEBS Lett., 72, 323 (1976). 2. Brown, M.S. et al., J. Biol. Chem., 253, 1121 (1978). 3....
Data Sheet - G5163
(1996). 7. Karlsen, A. E., et al., Proc. Natl. Acad. Sci., 88, 8337 (1991). 8. Michelsen, B. K., et al., Proc. Natl. Acad. Sci., 88, 8754 (1991). 9. Kaufman, D. L. et al., J. Neurochem., 56
Data Sheet - G4913
593 (1996) 7. Karlsen, A.E., et al., Proc. Natl. Acad. Sci., 88, 8337 (1991) 8. Michelsen, B.K., et al., Proc. Natl. Acad. Sci., 88, 8754 (1991) 9. Kaufman, D.L. et al, J. Neurochem. 56, 720
Data Sheet - N6539
corresponding sequence is identical in human NUMB isoforms 1-4 and in mouse NUMB, and is highly conserved (88% identity) in rat NUMB. The antibody is affinity-purified using the immunizing peptide immobilized
Data Sheet - G5038
(1996). 7. Karlsen, A.E., et al., Proc. Natl. Acad. Sci., 88, 8337 (1991). 8. Michelsen, B.K., et al., Proc. Natl. Acad. Sci., 88, 8754 (1991). 9. Kaufman, D.L. et al., J. Neurochem. 56, 720
Data Sheet - G5419
(1996). 9. Karlsen, A.E., et al., Proc. Natl. Acad. Sci., 88, 8337 (1991). 10. Michelsen, B.K., et al., Proc. Natl. Acad. Sci., 88, 8754 (1991). 11. Kaufman, D.L., et al., J. Neurochem., 56
Data Sheet - P1374
produced in rabbit using a peptide, (C)DEDQKVRPNEENNKDAD, corresponding to amino acid residues 72-88 of human BDNF (precursor) as the immunogen. This sequence has 16/17 residues identical in mouse
Data Sheet - G4388
bloodstream form of Trypanosoma brucei.2 Molecular weight:3 131 kDa (gel filtration, sucrose density centrifugation) GPO is a dimeric protein with two 72 kDa subunits.3 Cofactor:4 FAD Optimum
Data Sheet - P5999
Bell, J.E., In: Prion Diseases, Eds.: Collinge, J., and Palmer, M.S., p. 57-88, Oxford University Press (1997). 2. Prusiner, S.B., et al., Science, 252, 1515-1522 (1991). 3. Prusiner, S.B.
Data Sheet - M5302
cross-react with other MMP family members (MMP-1, MMP-2, MMP-3, etc). By immunoblotting against the reduced protein, the antibody reacts with bands at 92 kD and 88 kD (the proform and active form). It does not
Data Sheet - M5177
cross-react with other MMP family members (MMP-1, MMP-2, MMP-3, etc). By immunoblotting against the reduced protein, the antibody reacts with bands at 92 kDa and 88 kDa (the proform and active form). It does
Product Information Sheet - M4809
active enzyme and TIMP present. The following bands may be detected: MMP-9 Proenzyme (>85%) at ∼88 kDa non-reduced and 92 kDa reduced minor band (MMP-9 dimer) at ∼180 kDa intermediate active
Product Information Sheet - A2263
ADDITIONAL REFERENCES / REVIEW ARTICLES: Faulstich, H., Progress in Molecular & Subcellular Biology, 7, 88-134 (1980). "The Amatoxins." Zahler, A.M. and Prescott, D.M., Nucleic Acids Research, 17, 6299-6317
Product Information Sheet - C8982
Bradykinin fragment 1-7 757.3997 (Mono) KNG_HUMAN C35H53N10O9 α-cyano A8846 [68521-88-0] Angiotensin II (human) 1,046.5423 (Mono) ANGT_HUMAN C50H72N13O12 α-cyano P2613 P14R
Product Information Sheet - S8313
Bradykinin fragment 1-7 757.3997 (Mono) KNG_HUMAN C35H53N10O9 α-cyano A8846 [68521-88-0] Angiotensin II (human) 1,046.5423 (Mono) ANGT_HUMAN C50H72N13O12 α-cyano P2613 P14R
HandyStep Electronic Pipette Leaflet
84 7026 84 7023 70 1,0 100 7024 36 7026 85 7024 06 1,25 100 7023 86 7026 86 7023 72 2,5 100 7023 88 7026 88 7023 74 5,0 100 7023 90 7026 90 7023...
Data Sheet - M9555
MMP-1, MMP-2, MMP-3, MMP-8, etc). Anti-MMP-9 recognizes both native and reduced forms of MMP-9. By immunoblotting against the reduced human protein, the antibody detects bands at 92 kDa and 88 kDa (the pro-form
Data Sheet - P1115
Diseases. In Prion Diseases, Collinge, J. and Palmer, M. S. (Eds.) pp. 57-88 (Oxford University Press, 1997). 2. Prusiner, S. B., et al., Science, 252, 1515-1522 (1991). 3. Prusiner, S.

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