MARCKS(phospho-Ser170) Antibody

Description

Product Name MARCKS(phospho-Ser170) Antibody
Host Species Rabbit
Clonality Polyclonal
Purification Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Applications WB IHC
Species Reactivity Hu
Specificity The antibody detects endogenous level of MARCKS only when phosphorylated at threonine 170.
Immunogen Type Peptide-KLH
Immunogen Description Peptide sequence around phosphorylation site of Serine 170 (G-F-S(p)-F-K) derived from Human MARCKS.
Target Name MARCKS
Modification Phospho-Ser170
Alternative Names MACS, 80K-L, PKCSL, PRKCSL
Accession No. Swiss-Prot: P29966
NCBI Protein: NP_002347.5
Concentration 1.0mg/ml
Formulation Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Storage Store at -20°C for long term preservation (recommended). Store at 4°C for short term use.

Application Details

Predicted MW: 80kd
Western blotting: 1:500~1:1000
Immunohistochemistry: 1:50~1:100

Images

Western blot analysis of extracts from MCF cells untreated or treated with EGF using MARCKS(phospho-Ser170) Antibody #AB11535.
Immunohistochemical analysis of paraffin-embedded human lung carcinoma tissue using MARCKS(Phospho-Ser170) Antibody #AB11535(left) or the same antibody preincubated with blocking peptide(right).
Western blot analysis of extracts from 3T3 cells, treated with serum or calf intestinal phosphatase (CIP), using MARCKS (phospho-Ser170) Antibody #AB11535.

Background

MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.

Ramsden, J.J. (2000) Int. J. Biochem. Cell Biol. 32, 475-479.
Graff, J. M. et al. (1989) J. Biol. Chem. 264, 21818-21823.
Hartwig, J. H. et al. (1992) Nature 356, 618-622.
Thelen, M. et al. (1991) Nature 351, 320-322.

Published Papers

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