Product: Phospho-CD227/MUC1 (Tyr1229) Antibody
Catalog: AF0037
Source: Rabbit
Application: WB, IHC, IF/ICC, ELISA(peptide)
Reactivity: Human, Mouse
Mol.Wt.: 170kD; 122kD(Calculated).
Uniprot: P15941
RRID: AB_2834086

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Reactivity:
Human,Mouse
Clonality:
Polyclonal
Specificity:
Phospho-CD227/MUC1 (Tyr1229) Antibody detects endogenous levels of CD227/MUC1 only when phosphorylated at Tyrosine 1229.
RRID:
AB_2834086
Cite Format: Affinity Biosciences Cat# AF0037, RRID:AB_2834086.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

ADMCKD; ADMCKD1; Breast carcinoma associated antigen DF3; Breast carcinoma-associated antigen DF3; CA 15-3; CA15 3; CA15 3 antigen; CA15.3; Cancer antigen 15-3; Carcinoma associated mucin; Carcinoma-associated mucin; CD 227; CD227; DF3 antigen; EMA; Episialin; H23 antigen; H23AG; KL 6; KL-6; KL6; Krebs von den Lungen-6; MAM 6; MAM6; MCD; MCKD; MCKD1; Medullary cystic kidney disease 1 (autosomal dominant); Medullary cystic kidney disease, autosomal dominant; MUC 1; MUC-1; MUC-1/SEC; MUC-1/X; MUC1; MUC1-alpha; MUC1-beta; MUC1-CT; MUC1-NT; MUC1/ZD; MUC1_HUMAN; Mucin 1; Mucin 1 transmembrane; Mucin 1, cell surface associated; Mucin-1 subunit beta; Peanut reactive urinary mucin; Peanut-reactive urinary mucin; PEM; PEMT; Polymorphic epithelial mucin; PUM; Tumor associated epithelial membrane antigen; Tumor associated epithelial mucin; Tumor associated mucin; Tumor-associated epithelial membrane antigen; Tumor-associated mucin;

Immunogens

Immunogen:

A synthesized peptide derived from human CD227/MUC1 around the phosphorylation site of Tyr1229.

Uniprot:
Gene(ID):
Expression:
P15941 MUC1_HUMAN:

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.

Description:
This gene is a member of the mucin family and encodes a membrane bound, glycosylated phosphoprotein. This protein is anchored to the apical surface of many epithelia by a transmembrane domain, with the degree of glycosylation varying with cell type. The protein serves a protective function, binding to pathogens, as well as functioning in a cell signaling capacity. Overexpression, aberrant intracellular localization, and changes in glycosylation of this protein have been associated with carcinomas. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Sequence:
MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDNRPALGSTAPPVHNVTSASGSASGSASTLVHNGTSARATTTPASKSTPFSIPSHHSDTPTTLASHSTKTDASSTHHSSVPPLTSSNHSTSPQLSTGVSFFFLSFHISNLQFNSSLEDPSTDYYQELQRDISEMFLQIYKQGGFLGLSNIKFRPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL

PTMs - P15941 As Substrate

Site PTM Type Enzyme
T131 O-Glycosylation
T139 O-Glycosylation
S989 O-Glycosylation
T990 O-Glycosylation
S993 O-Glycosylation
S999 O-Glycosylation
T1001 O-Glycosylation
T1003 O-Glycosylation
T1004 O-Glycosylation
S1009 O-Glycosylation
T1010 O-Glycosylation
S1090 Phosphorylation
Y1191 Phosphorylation
T1202 Phosphorylation
Y1203 Phosphorylation P09619 (PDGFRB) , P43403 (ZAP70)
S1207 Phosphorylation
Y1209 Phosphorylation
T1211 Phosphorylation
Y1212 Phosphorylation
T1214 Phosphorylation
Y1218 Phosphorylation P09619 (PDGFRB)
S1222 Phosphorylation
S1223 Phosphorylation
T1224 Phosphorylation Q05655 (PRKCD)
S1227 Phosphorylation P49841 (GSK3B)
Y1229 Phosphorylation P00533 (EGFR) , P06239 (LCK) , P12931 (SRC) , P07948 (LYN)
S1233 Phosphorylation
S1240 Phosphorylation
S1242 Phosphorylation
Y1243 Phosphorylation A0A173G4P4 (Abl fusion)
T1244 Phosphorylation

Research Backgrounds

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.

PTMs:

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.

Subcellular Location:

Apical cell membrane>Single-pass type I membrane protein.
Note: 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.

Secreted.

Secreted.

Secreted.

Cell membrane. Cytoplasm. Nucleus.
Note: 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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.

Subunit Structure:

The alpha subunit forms a tight, non-covalent heterodimeric complex with the proteolytically-released beta-subunit. Interaction, via the tandem repeat region, with domain 1 of ICAM1 is implicated in cell migration and metastases. Isoform 1 binds directly the SH2 domain of GRB2, and forms a MUC1/GRB2/SOS1 complex involved in RAS signaling. The cytoplasmic tail (MUC1CT) interacts with several proteins such as SRC, CTNNB1 and ERBs. Interaction with the SH2 domain of CSK decreases interaction with GSK3B. Interacts with CTNNB1/beta-catenin and JUP/gamma-catenin and promotes cell adhesion. Interaction with JUP/gamma-catenin is induced by heregulin. Binds PRKCD, ERBB2, ERBB3 and ERBB4. Heregulin (HRG) stimulates the interaction with ERBB2 and, to a much lesser extent, the interaction with ERBB3 and ERBB4. Interacts with P53 in response to DNA damage. Interacts with KLF4. Interacts with estrogen receptor alpha/ESR1, through its DNA-binding domain, and stimulates its transcription activity. Binds ADAM17. Isoform ZD forms disulfide-linked oligomers.

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