MUC1 Blocking Peptide for STJ501818 peptide (STJ504390)

SKU:
STJ504390-250

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Applications: Immunodepletion/Immunocompetition
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: MUC1 Blocking Peptide for STJ501818 is synthetically produced from the sequence and is suitable for use in western blot applications.
Formulation: Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice.
Dilution Range: WB:
IHC: 1:200
ICC: 1:200
IF: 1:200
CFM: 1:200
Storage Instruction: Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Gene Symbol: MUC1
Gene ID: 4582
Uniprot ID: MUC1_HUMAN
Specificity: This blocking peptide is recommended for use in combination with MUC1 antibody, STJ501818
Immunogen: Synthetic peptide corresponding to unique amino acid sequence on MUCIN1 protein.
Tissue Specificity Expressed on the apical surface of epithelial cells, especially of airway passages, breast and uterus. Also expressed in activated and unactivated T-cells. Overexpressed in epithelial tumors, such as breast or ovarian cancer and also in non-epithelial tumor cells. Isoform Y is expressed in tumor cells only.
Post Translational Modifications Highly glycosylated (N- and O-linked carbohydrates and sialic acid). O-glycosylated to a varying degree on serine and threonine residues within each tandem repeat, ranging from mono- to penta-glycosylation. The average density ranges from about 50% in human milk to over 90% in T47D breast cancer cells. Further sialylation occurs during recycling. Membrane-shed glycoproteins from kidney and breast cancer cells have preferentially sialyated core 1 structures, while secreted forms from the same tissues display mainly core 2 structures. The O-glycosylated content is overlapping in both these tissues with terminal fucose and galactose, 2- and 3-linked galactose, 3- and 3,6-linked GalNAc-ol and 4-linked GlcNAc predominating. Differentially O-glycosylated in breast carcinomas with 3,4-linked GlcNAc. N-glycosylation consists of high-mannose, acidic complex-type and hybrid glycans in the secreted form MUC1/SEC, and neutral complex-type in the transmembrane form, MUC1/TM. Proteolytic cleavage in the SEA domain occurs in the endoplasmic reticulum by an autoproteolytic mechanism and requires the full-length SEA domain as well as requiring a Ser, Thr or Cys residue at the P + 1 site. Cleavage at this site also occurs on isoform MUC1/X but not on isoform MUC1/Y. Ectodomain shedding is mediated by ADAM17. Dual palmitoylation on cysteine residues in the CQC motif is required for recycling from endosomes back to the plasma membrane. Phosphorylated on tyrosines and serine residues in the C-terminal. Phosphorylation on tyrosines in the C-terminal increases the nuclear location of MUC1 and beta-catenin. Phosphorylation by PKC delta induces binding of MUC1 to beta-catenin/CTNNB1 and thus decreases the formation of the beta-catenin/E-cadherin complex. Src-mediated phosphorylation inhibits interaction with GSK3B. Src- and EGFR-mediated phosphorylation on Tyr-1229 increases binding to beta-catenin/CTNNB1. GSK3B-mediated phosphorylation on Ser-1227 decreases this interaction but restores the formation of the beta-cadherin/E-cadherin complex. On T-cell receptor activation, phosphorylated by LCK. PDGFR-mediated phosphorylation increases nuclear colocalization of MUC1CT and CTNNB1. The N-terminal sequence has been shown to begin at position 24 or 28.
Function The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack. The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylations and protein-protein interactions. Modulates signaling in ERK, SRC and NF-kappa-B pathways. In activated T-cells, influences directly or indirectly the Ras/MAPK pathway. Promotes tumor progression. Regulates TP53-mediated transcription and determines cell fate in the genotoxic stress response. Binds, together with KLF4, the PE21 promoter element of TP53 and represses TP53 activity.
Peptide Name Mucin-1
Muc-1
Breast Carcinoma-Associated Antigen Df3
Cancer Antigen 15-3
Ca 15-3
Carcinoma-Associated Mucin
Episialin
H23ag
Krebs Von Den Lungen-6
Kl-6
Pemt
Peanut-Reactive Urinary Mucin
Pum
Polymorphic Epithelial Mucin
Pem
Tumor-Associated Epithelial Membrane Antigen
Ema
Tumor-Associated Mucin
Cd Antigen Cd227 Cleaved Into - Mucin-1 Subunit Alpha
Muc1-Nt
Muc1-Alpha - Mucin-1 Subunit Beta
Muc1-Beta
Muc1-Ct
Database Links Reactome: R-HSA-5083625
Reactome: R-HSA-5083632
Reactome: R-HSA-5083636
Reactome: R-HSA-5621480
Reactome: R-HSA-6785807
Reactome: R-HSA-913709
Reactome: R-HSA-977068
Cellular Localisation Apical Cell Membrane
Single-Pass Type I Membrane Protein
Exclusively Located In The Apical Domain Of The Plasma Membrane Of Highly Polarized Epithelial Cells
After Endocytosis
Internalized And Recycled To The Cell Membrane
Located To Microvilli And To The Tips Of Long Filopodial Protusions
Isoform 5: Secreted
Isoform Y: Secreted
Isoform 9: Secreted
Mucin-1 Subunit Beta: Cell Membrane
Cytoplasm
Nucleus
On Egf And Pdgfrb Stimulation
Transported To The Nucleus Through Interaction With Ctnnb1
A Process Which Is Stimulated By Phosphorylation
On Hrg Stimulation
Colocalizes With Jup/Gamma-Catenin At The Nucleus
Alternative Peptide Names Mucin-1 protein
Muc-1 protein
Breast Carcinoma-Associated Antigen Df3 protein
Cancer Antigen 15-3 protein
Ca 15-3 protein
Carcinoma-Associated Mucin protein
Episialin protein
H23ag protein
Krebs Von Den Lungen-6 protein
Kl-6 protein
Pemt protein
Peanut-Reactive Urinary Mucin protein
Pum protein
Polymorphic Epithelial Mucin protein
Pem protein
Tumor-Associated Epithelial Membrane Antigen protein
Ema protein
Tumor-Associated Mucin protein
Cd Antigen Cd227 Cleaved Into - Mucin-1 Subunit Alpha protein
Muc1-Nt protein
Muc1-Alpha - Mucin-1 Subunit Beta protein
Muc1-Beta protein
Muc1-Ct protein
MUC1 protein
PUM protein

Information sourced from Uniprot.org

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