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Human Mucin-1 / MUC-1 (890-1158) Protein, His Tag (MALS verified)

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分子别名(Synonym)

Mucin 1,MUC1,CD227,EMA,H23AG,KL-6,MAM6,MUC-1,SEC,MUC-1,X,MUC1,ZD,PEM,PEMT,PUM,CA15-3,Episialin

表达区间及表达系统(Source)

Human Mucin-1 (890-1158), His Tag (MU1-H52H9) is expressed from human 293 cells (HEK293). It contains AA Ser 890 - Gly 1158 (Accession # P15941-1).

Predicted N-terminus: Ser 890 (partial α chain) & Ser 1098 (partial β chain)

Request for sequence

蛋白结构(Molecular Characterization)

Mucin-1 Structure

This protein carries a polyhistidine tag at the C-terminus. The mature form of Mucin-1 is a non-covalent heterodimeric complex with the proteolytically cleaved partial α and partial β chain. Each partial α and partial β chain has a calculated MW of 21.3 kDa (partial α chain) and 8.4 kDa (partial β chain). The protein migrates as 40-80 kDa (partial glycosylated α chain) and 10 kDa (partial β chain) when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

内毒素(Endotoxin)

Less than 1.0 EU per μg by the LAL method.

纯度(Purity)

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

制剂(Formulation)

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

Contact us for customized product form or formulation.

重构方法(Reconstitution)

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

存储(Storage)

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:

  1. -20°C to -70°C for 12 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

Mucin-1 SDS-PAGE

Human Mucin-1 (890-1158), His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-MALS

Mucin-1 SEC-MALS

The purity of Human Mucin-1 (890-1158), His Tag (Cat. No. MU1-H52H9) is more than 90% and the molecular weight of this protein is around 40-55 kDa verified by SEC-MALS.

Report

 

活性(Bioactivity)-ELISA

Mucin-1 ELISA

Immobilized Human Mucin-1 / MUC-1 (890-1158) Protein, His Tag (Cat. No. MU1-H52H9) at 1 μg/mL (100 μL/well) can bind Anti-Mucin-1 Antibody, Mouse IgG1 with a linear range of 0.4-6 ng/mL (QC tested).

Protocol

 
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ACRO质量管理体系
 
 

背景(Background)

Membrane mucins have several functions in epithelial cells including cytoprotection, extravasation during metastases, maintenance of luminal structure, and signal transduction. MUC17, contains an extended, repetitive extracellular glycosylation domain and a carboxyl terminus with two EGF-like domains, a SEA module domain, a transmembrane domain, and a cytoplasmic domain with potential serine and tyrosine phosphorylation sites. Interacts via its C-terminus with PDZK1 and this interaction appears important for proper localization. Probably plays a role in maintaining homeostasis on mucosal surfaces.

 

前沿进展

Establishment of primary cell cultures from canine mammary gland malignant tumours: a preliminary study
Petrouškova, Hudáková, Almášiová et al
J Vet Res (2025) 69 (1), 159-168
Abstract: Canine mammary gland cancer (CMGC) is the most common neoplastic condition in bitches and is often fatal. There are limited treatment options for CMGC. Primary cell cultures from mammary tumours are promising preclinical in vitro models in which to study personalised treatment approaches. This preliminary study aimed to establish primary cell cultures from two canine mammary gland neoplasms: a common solid adenocarcinoma and a rare carcinosarcoma.Tumour masses were collected from a 13-year-old and a 16-year-old German shepherd. Tumour cells were isolated by mechanical disaggregation and enzymatic digestion of masses with 0.05% type IV collagenase. Primary cell cultures were validated by immunocytochemistry for specific markers including mucin 1 (MUC1), cytokeratin 8 and 18 (CK8/18) and Kiel 67 (Ki-67).Primary cell cultures achieved confluency by day 7 of culture, displaying polygonal cellular morphology. Cultures of both cell types exhibited strong positivity for MUC1 of >99% and high Ki-67 proliferation activity of 43.1% ± 0.5% in the solid adenocarcinoma-derived positive cells and 87.9% ± 2.7% in the carcinosarcoma-derived positive cells. Positivity was observed for CK8/18 of 98.1% ± 0.3% in cells derived from solid adenocarcinoma and 31.6% ± 1.5% in cells derived from carcinosarcoma.With further characterisation, the primary cell cultures established in this study can be expected to show considerable potential as foundational in vitro models for cancer research.© 2025 Patŕicia Petrouškova et al., published by Sciendo.
New Radiopharmaceutical Tracers in Breast Cancer Diagnosis and Therapy
Rahmati, Mousavi, Souri et al
Anticancer Agents Med Chem (2025)
Abstract: Breast cancer (BC) remains a predominant cause of mortality among women, with early diagnosis and ongoing monitoring being crucial for effective management. Integrating nuclear medicine with radiological modalities offers non-invasive anatomical and functional information, enabling precise target localization and quantification. This approach guided the selection of the most appropriate personalized treatment and predicted its efficacy, reducing the use of unnecessary drugs and lowering patient management costs. Since 2020, significant breakthroughs have been made in the development of radiopharmaceuticals, which are different in importantly targeting agents and radionuclides, with a focus on their efficacy in preclinical studies. This review accentuates the central role of radiopharmaceuticals in recent advancements for both imaging and therapeutic applications in BC. We discussed various receptor-targeted radiopharmaceutical therapy (RPT) agents currently utilized in clinical and preclinical settings with their chemical structures, along with the challenges faced in their implementation, including angiotensin II type 1 receptor (AT1 receptor), integrins αvβ3, chemokine receptor (CXCR4), and trophoblast cell-surface antigen-2 (TROP2), cyclin-dependent kinases 4 and 6 (CDK4/6) inhibitor, and epithelial cell adhesion molecule (EpCAM)-targeted, epidermal growth factor receptor (EGFR), vascular endothelial growth factor receptor (VEGFR), fibroblast activation protein inhibitor (FAPI), and mucin 1 (MUC1). While numerous promising RPT agents were still in preclinical stages, this review underscored the potential of tailored radiopharmaceuticals to enhance BC diagnosis and treatment, providing novel avenues for personalized medicine.Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.
Study on the Construction and Anti-Tumor Effect of aPDL1/aMUC1 Double Antibody Modification of Doxorubicin Liposome
Zhao, Xuan, Diao et al
ACS Omega (2025) 10 (10), 10107-10121
Abstract: In recent years, the primary treatments for cancer have included chemotherapy, radiotherapy, and surgery. However, challenges such as poor prognosis, high recurrence rates, low survival rates, and diminished quality of life persist in cancer management. Recently, immunotherapy has emerged as a potent therapeutic approach for treating tumors. To this end, we developed antibodies for mucin 1 (MUC1) and programmed cell death ligand 1 (PD-L1) to functionalize liposomes and incorporate doxorubicin (DOX) (DOX-aMUC1/aPDL1-Lip). This formulation is designed to enhance its targeting capability and antitumor activity against cancer cells. The DOX-aMUC1/aPDL1-Lip formulation demonstrated significant antitumor effects both in vivo and in vitro, effectively inhibiting tumor cell growth. Utilizing antibodies against PD-L1 and MUC1 to modify liposomes represents a novel strategy for cancer treatment.© 2025 The Authors. Published by American Chemical Society.
Filter-Assisted ICP-MS Tumor Liquid Biopsy Enabled by Dual-Target-Regulated Functional DNA Nanospheres Cascade Amplification
Wu, Wang, Yan et al
Small Methods (2025)
Abstract: An ultrasensitive ICP-MS aptasensor is developed utilizing a label-free, simple filter membrane-assisted separation technique combined with nucleic acid signal amplification for the analysis of circulating tumor cells (CTCs) in lung cancer clinical samples. The approach is based on the high-affinity interaction between aptamers and PD-L1 and mucin 1, which are overexpressed on the cell surface, in conjunction with functional Y-DNA nanospheres and catalytic hairpin assembly amplifications, enabling the simultaneous detection of two proteins. Additionally, a four-armed nanostructure with significant spatial site resistance is self-assembled by introducing streptavidin with biotinylated-hairpin structures, improving the separation efficiency of the filter membrane. This structural design enables the effective isolation of biotin-T-Hg2+-T and biotin-C-Ag+-C from free Hg2+ and Ag+, facilitating highly sensitive dual-protein detection via ICP-MS. The limits of detection reached ag mL-1 levels for proteins and single-cell levels for A549 cells. CTCs are extracted from whole blood samples of lung cancer patients within 45 min through a simple centrifugation procedure. Quantification of CTCs is performed in 37 clinical samples, demonstrating results consistent with clinical diagnoses. The assay exhibits a specificity of 100% and a sensitivity of 94.5%.© 2025 Wiley‐VCH GmbH.
Showing 1-4 of 7621 papers.
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Mucin-1靶点信息
英文全称:Mucin-1
中文全称:黏蛋白-1
种类:Homo sapiens
上市药物数量:0详情
临床药物数量:22详情
最高研发阶段:临床二期
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