WH0004082M6
Monoclonal Anti-MARCKS antibody produced in mouse
clone 2C2, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-80KL, Anti-FLJ14368, Anti-MACS, Anti-MRACKS, Anti-PKCSL, Anti-PRKCSL, Anti-myristoylated alanine-rich protein kinase C substrate
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2C2, monoclonal
form
buffered aqueous solution
species reactivity
mouse
technique(s)
immunofluorescence: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL
isotype
IgG1κ
GenBank accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MARCKS(4082)
Related Categories
General description
Myristoylated alanine-rich C-kinase substrate (MARCKS) contains an N-terminal domain (ND), effector domain (ED), and myristoylated MH2 domain. The MARCKS gene is mapped to human chromosome 6q21.
Immunogen
MARCKS (NP_002347, 2 a.a. ~ 65 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
GAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAP
Sequence
GAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAP
Application
Monoclonal Anti-MARCKS antibody produced in mouse has been used in immunohistochemistry (1:400).
Biochem/physiol Actions
Myristoylated alanine-rich C-kinase substrate (MARCKS) is involved in mediating brain plasticity, inflammatory response, embryonic development, and regeneration processes. It also plays a key role in cell cycle regulation and transmembrane transport. Various studies have implicated the association of MARCKS with the pathophysiology of glioblastoma, cholangiocarcinoma, melanoma, and many more tumor types.
Physical form
Solution in phosphate buffered saline, pH 7.4
Legal Information
GenBank is a registered trademark of United States Department of Health and Human Services
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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John J Park et al.
Oncogenesis, 13(1), 9-9 (2024-02-29)
Protein kinase C (PKC) is activated downstream of gain-of-function GNAQ or GNA11 (GNAQ/GNA11) mutations in over 90% of uveal melanoma (UM). Phase I clinical trials of PKC inhibitors have shown modest response rates with no survival benefit in metastatic UM.
Hervé Ghesquieres et al.
Journal of clinical oncology : official journal of the American Society of Clinical Oncology, 33(33), 3930-3937 (2015-10-16)
We performed a multistage genome-wide association study to identify inherited genetic variants that predict outcome in diffuse large B-cell lymphoma patients treated with immunochemotherapy. We conducted a meta-analysis of two genome-wide association study data sets, one from the LNH2003B trial
Mohamed El Amri et al.
Journal of biomedical science, 25(1), 43-43 (2018-05-24)
The Myristoylated Alanine-Rich C-kinase Substrate (MARCKS) and MARCKS-like protein 1 (MARCKSL1) have a wide range of functions, ranging from roles in embryonic development to adult brain plasticity and the inflammatory response. Recently, both proteins have also been identified as important
Krista Rombouts et al.
Cancer letters, 333(2), 244-252 (2013-02-05)
Several actin-binding proteins have been shown to be altered in metastatic cell lines and tumours and, in particular, Myristoylated Alanine-Rich protein Kinase C substrate (MARCKS) has been implicated in the pathogenesis of various highly metastatic epithelial malignancies. Considering that a
Takeyuki Sugawara et al.
Proceedings of the National Academy of Sciences of the United States of America, 114(26), E5256-E5265 (2017-06-14)
Dendritic spines of Purkinje cells form excitatory synapses with parallel fiber terminals, which are the primary sites for cerebellar synaptic plasticity. Nevertheless, how density and morphology of these spines are properly maintained in mature Purkinje cells is not well understood.
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