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48-602MAG
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Anti-MBP (Citrulline R122), clone 1H1, Cat. No. MABT1499, is a mouse monoclonal antibody that detects Myelin basic protein citrullinated on residue 122 and has been is tested for use in ELISA, Immunohistochemistry, and Western Blotting.
More>>Anti-MBP (Citrulline R122), clone 1H1, Cat. No. MABT1499, is a mouse monoclonal antibody that detects Myelin basic protein citrullinated on residue 122 and has been is tested for use in ELISA, Immunohistochemistry, and Western Blotting. Less<<
Myelin basic protein (UniProt: P02686; also known as MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein) is encoded by the MBP gene (Gene ID: 4155) in human. MBP is a homodimeric protein that is found in both the central and the peripheral nervous system. It is one of the most abundant protein component of the myelin membrane in the CNS and plays a role in both the formation and stabilization of this myelin membrane. It is responsible for adhesion of the cytosolic surfaces of multilayered compact myelin. MBP can interact with many polyanionic proteins including actin, tubulin, calmodulin, and clathrin, and with negatively charged lipids. MBP isoforms are found in both the central and the peripheral nervous system, whereas Golli-MBP isoforms are expressed in fetal thymus, spleen and spinal cord, as well as in cell lines derived from the immune system. MBP expression begins abruptly in 14-16-week-old fetuses. Even smaller isoforms seem to be produced during embryogenesis; some of these persisting in the adult. MBP citrullination by peptidylarginine deiminase (PAD) leads to incomplete protein-lipid bilayer interactions and increases its vulnerability to proteolytic enzymes, resulting in disorganization of the myelin sheath in the central nervous system. Citrullinated MBP (citMBP) has been suggested to be a hallmark of demyelination. MBP citrullination has frequently been demonstrated in various CNS disorders. citMBP at R25, R122, and R130 is reported in the brains of subjects with Creutzfeldt-Jakob disease (CJD). Clone 1H1 specifically recognizes citMBP at R122. (Ref.: Jang, B., et al. (2017). Mol. Neurobiol. 55(4); 3172-3184; Boggs, JM (2006). Cell. Mol. Life Sci. 63(17); 1945-1961).
References
Product Information
Format
Purified
Presentation
Purified mouse monoclonal antibody IgG1 in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Applications
Application
Anti-MBP (Citrulline R122), clone 1H1, Cat. No. MABT1499, is a mouse monoclonal antibody that detects Myelin basic protein citrullinated on residue 122 and has been is tested for use in ELISA, Immunohistochemistry, and Western Blotting.
Key Applications
ELISA
Western Blotting
Immunohistochemistry
Application Notes
ELISA Analysis: A representative lot detected MBP (Citrulline R122) in ELISA applications (Jang, B., et. al. (2018). Mol Neurobiol. 55(4):3172-3184).
Western Blotting Analysis: A representative lot detected MBP (Citrulline R122) in Western Blotting applications (Jang, B., et. al. (2018). Mol Neurobiol. 55(4):3172-3184).
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected MBP (Citrulline R122) in Myelin basic protein (MBP) treated with human PAD2 (Courtesy of Byungki Jang, Ph.D./Eun-Kyoung Choi, Ph.D., Ilsong Institute of Life Science, Hallym University, South Korea).
Immunohistochemistry Analysis: A representative lot detected MBP (Citrulline R122) in Immunohistochemistry applications (Jang, B., et. al. (2018). Mol Neurobiol. 55(4):3172-3184).
(Courtesy of Byungki Jang, Ph.D./Eun-Kyoung Choi, Ph.D., Ilsong Institute of Life Science, Hallym University, South Korea).
Biological Information
Immunogen
KLH-conjugated linear peptide corresponding to 19 amino acids from isoform 5 of human Myelin Basic Protein with citrullination on residue 122.
Clone
1H1
Concentration
Please refer to lot specific datasheet.
Host
Mouse
Specificity
Clone 1H1 is a mouse monoclonal antibody that detects human and murine myelin basic protein citrullinated on residue 122. It targets an epitope with in 19 amino acids from the C-terminal half.
~41 kDa observed; 18.59 kDa calculated. Uncharacterized bands may be observed in some lysate(s).
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in GST-tagged myelin basic protein (MBP) treated with human PAD-2.
Western Blotting Analysis: 1 µg/mL of this antibody detected MBP (Citrulline R122) in GST-tagged myelin basic protein (MBP) treated with human Peptidyl Arginine Deiminase 2 (PAD-2)(200 ng for 4 h at 37°C).
Usage Statement
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.
Keratins (K) are intermediate filament proteins important in stress protection and mechanical support of epithelial tissues. K8, K18 and K19 are the main colonic keratins, and K8-knockout (K8-/-) mice display a keratin dose-dependent hyperproliferation of colonic crypts and a colitis-phenotype. However, the impact of the loss of K8 on intestinal cell differentiation has so far been unknown. Here we show that K8 regulates Notch1 signalling activity and differentiation in the epithelium of the large intestine. Proximity ligation and immunoprecipitation assays demonstrate that K8 and Notch1 co-localize and interact in cell cultures, and in vivo in the colonic epithelial cells. K8 with its heteropolymeric partner K18 enhance Notch1 protein levels and activity in a dose dependent manner. The levels of the full-length Notch1 receptor (FLN), the Notch1 intracellular domain (NICD) and expression of Notch1 downstream target genes are reduced in the absence of K8, and the K8-dependent loss of Notch1 activity can be rescued with re-expression of K8/K18 in K8-knockout CRISPR/Cas9 Caco-2 cells protein levels. In vivo, K8 deletion with subsequent Notch1 downregulation leads to a shift in differentiation towards a goblet cell and enteroendocrine phenotype from an enterocyte cell fate. Furthermore, the K8-/- colonic hyperproliferation results from an increased number of transit amplifying progenitor cells in these mice. K8/K18 thus interact with Notch1 and regulate Notch1 signalling activity during differentiation of the colonic epithelium.
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