Immunoprecipitation assay

Das PM, Ramachandran K, vanWert J, Singal R. 2004. Chromatin immunoprecipitation assay. Biotechniques 37 961-969. 

Hanna PA, Jankovic J, Vincent A (1999) Comparison of mouse bioassay and immunoprecipitation assay for botulinum toxin antibodies. J Neurol Neurosurg Psychiatry 66 612-16 Hanson MA, Stevens RC (2000) Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution. Nat Struct Biol 7 687-92 Harlow ML, Ress D, Stoschek A, Marshall RM, McMahan UJ (2001) The architecture of active zone material at the frog s neuromuscular junction. Nature 409 479-84 Harris JB (1997) Toxic phospholipases in snake venom an introductory review. Symp. zool. Soc. Lond. 70 235-50... 

CK-MB can be measured in numerous ways. Immunoassays developed in recent years have improved on the analytical and clinical sensitivity and specificity of the earlier immunoinhibition and immunoprecipitation assays. These assays now (1) measure CK-MB directly and provide mass measurements, (2) are easily automated, and (3) provide rapid results (<30 minutes). Mass assays reliably measure low CK-MB concentrations in both samples with low total enzyme activity (<100 U/L) and with high total enzyme activity (>10,000 U/L). Furthermore, no interferences from other proteins have been documented. The majority of commercially available immunoassays that use monoclonal anti-CK-MB antibodies are the same as those listed in Table 5-2 for cardiac troponin assays. Excellent concordance has been shown between mass concentration and activity assays. A primary reference material is commercially available to assist in harmonization. If used for assay standardization, then this material allows... 

Current data from in vitro DNA binding assays and transfection experiments point to Nrf2 as the most important protein involved in stimulating ARE-driven transcription. Using the chromatin immunoprecipitation assay (ChIP) studies from... 

Figure 4.3. Map of alanine substitution in hGH disrupt binding of hGHbp at either site 1 or site 2. The two sites are generally delieated by the large shaded circles. Residues for which alanine mutations reduce site 2 binding are shown , 2- to 4-fold FA, 4- to 10-fold 10- to 50-fold and FA, >50-fold. Sites where alanine mutations in site 1 cause changes in binding affinity for the hGHbp using an immunoprecipitation assay, are shown , 2- to 4-fold reduction , 4- to 10-fold reduction > 10-fold reduction and, 4-fold increase.

Antibody G6 bound to the native enzyme with an affinity similar to antibody D4 as shown by the indirect immunoprecipitation assay in Fig. 2. The immune complex of antibody G6 and the enzyme adsorbed to protein A-Sepharose exhibited enzyme activity approximately 40% of the immunoprecipitated enzyme activity that was removed from the supernatant fraction was recovered in the pellet fraction. The immune complex of antibody D4 did not show enzyme activity. Antibody X3 did not remove... 

Detection limits of the ligand-binding immunoprecipitation assay are about 5 fmol receptor /mg total-soluble protein, using the tritiated ligands now available that have specific activities of -28-50 Ci/mmol. The production of ligands with higher specific activities will increase the detection limit and/or help to reduce the amount of protein extract that is required per assay point... 

The maximum efficiency of the ligand-binding immunoprecipitation assay that we have achieved is about 80-90%, as determined by calculation of the amount... 

FIGURE 5 Immunoprecipitation of the autoantigen fibrillarin using autoantibodies. cDNA encoding mouse fibrillarin was radiolabeled with [35S]methionine by in vitro transcription and translation (TnT mFIB). This protein was then used in a protein A-Sepharose bead immunoprecipitation assay to examine human sera (A-L) for antifibrillarin antibodies. Positive sera are identified by an asterisk. POS. CONT, immunoprecipitate from an antifibrillarin-positive serum NEG. CONT, immunoprecipitate from an antifibrillarinnegative serum. 

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