spectroscopy to assay for urease from
Pseudomonas aeruginosa and Canavalia
ensiformis. Anal. Biochem., 331, 115-21 (2004).
GY,KAD,RBG,JWM,MAM 03/14-1
2014 Sigma-Aldrich Co. LLC. All rights reserved.
spectroscopy to assay for urease from
Pseudomonas aeruginosa and Canavalia
ensiformis. Anal. Biochem., 331, 115-21 (2004).
GY,KAD,RBG,JWM,MAM 03/14-1
2014 Sigma-Aldrich Co. LLC. All rights reserved.
tunicamycin
on epidermal glycoprotein and glycosaminoglycan
synthesis in vitro. Biochem. J., 198(2), 331-338
(1981).
11. Maheshwari, R.K., et al., Tunicamycin enhances
the antiviral and anticellular
spectroscopy to assay for urease from
Pseudomonas aeruginosa and Canavalia
ensiformis. Anal. Biochem., 331, 115-21 (2004).
GY,KAD,RBG,JWM,MAM 03/14-1
2014 Sigma-Aldrich Co. LLC. All rights reserved.
spectroscopy to assay for urease from
Pseudomonas aeruginosa and Canavalia
ensiformis. Anal. Biochem., 331, 115-21 (2004).
GY,KAD,RBG,JWM,MAM 03/14-1
2014 Sigma-Aldrich Co. LLC. All rights reserved.
Enzymes of Molecular Biology, Burrell, M.M.,
ed. Humana Press Inc. Totowa, NJ 1993, Chapter
19, 331.
11. del C. Batlle, A.M. et al., Methods Enzymol., 17A,
216, 1970.
12. Mikami, B. et al.
Enzymes of Molecular Biology, Burrell, M.M.,
ed. Humana Press Inc. Totowa, NJ 1993, Chapter
19, 331.
11. del C. Batlle, A.M. et al., Methods Enzymol., 17A,
216, 1970.
12. Mikami, B. et al.
Prostaglandins and Cancer: First
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35. Kohler, P. et.al. (1968). Biochem
transferase of Escherichia coli. Location of the acetyl group. FEMS
Microbiology Letters 110, pp 331 – 334, 1993
K Smalla, R Prager, M Isemann, R Pukall, E Tietze, J.D. van Elsas, H Tschäpe, Distribution
Recognizes the ~110-116 kDa full length PARP and its ~85 kDa
cleaved fragment . ELISA, IB, IF
100 ml €331
Anti-PARP-1 (197-214) Rabbit pAb 512738 Undiluted serum . Immunogen used was a synthetic peptide
PE square box
Material: HDPE, white
Nominal volume: 35 L
Weight: min. 1.43 kg
Height: 331 mm
Width: 379 mm
Length: 379 mm
Closure
Material: PP
Primary packaging inside: PE
HDAC-6 H2287 10013 HDAC6 P NP_006035.2 y y n/d
330 HDAC-5 H4538 10014 HDAC5 M NP_001015053.1 y y y
331 HDAC-5 H8163 10014 HDAC5 P NP_001015053.1 y y y
71 Bim B7929 10018 BCL2L11 P NP_001191035.1 y y y
37
HDAC-6 H2287 10013 HDAC6 P NP_006035.2 y y n/d
330 HDAC-5 H4538 10014 HDAC5 M NP_001015053.1 y y y
331 HDAC-5 H8163 10014 HDAC5 P NP_001015053.1 y y y
71 Bim B7929 10018 BCL2L11 P NP_001191035.1 y y y
37
HDAC-6 H2287 10013 HDAC6 P NP_006035.2 y y n/d
330 HDAC-5 H4538 10014 HDAC5 M NP_001015053.1 y y y
331 HDAC-5 H8163 10014 HDAC5 P NP_001015053.1 y y y
71 Bim B7929 10018 BCL2L11 P NP_001191035.1 y y y
37
25029; Jourdain, L., et al.
1997. Biochemistry 36, 10817; Curmi, P.A., et al. 1994. Biochem J. 300, 331.
Tryprostatin A, Aspergillus fumigatus
A specific inhibitor
of microtubule-
associated protein
80 nM for IL-6,
110 nM for PGE2, and 210 nM for IL-8 and TNF-a), as well as LPS-induced NF-kB activation
(IC50 = 270 nM) and NO production (IC50 = 230 nM) in RAW264.7 cells. Preferentially
inhibits chymotrypsin-like