Mucin-7 Antibodies

Mucin-7 (MUC7)

May function in a protective capability by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.

aeruginosa pili. .

Gene Information

Human
Gene Name:	MUC7
Uniprot:	Q8TAX7
Entrez:	4589

Family

Belongs to:
No superfamily

Alternative Names

apo-MG2; DKFZp686J03256; FLJ27047; MG2MGC34772; MUC-7; mucin 7, secreted; mucin-7; Salivary mucin-7; salivary

Molecular Weight

Mass (kDA):
39.159 kDA

Genomic Context

Human
Location:	4q13.3
Sequence:	4; NC_000004.12 (70430492..70482997)

Tissue Specificity

Expressed in salivary gland tissues and only in those that contain mucous acinar cells (e.g. sublingual and submandibular glands) and not in salivary glands containing only serous acinar cells (e.g. parotid gland).

Subcellular Localizations

Secreted.

Diseases

• Mucinous Adenocarcinoma
• Salivary Gland Diseases
• Neoplasms
• Malignant Neoplasms
• Carcinoma
• Conjunctival Diseases
• Adenocarcinoma
• Malignant Paraganglionic Neoplasm
• Neoplasm Metastasis
• Bladder Neoplasm
• Malignant Neoplasm Of Urinary Bladder
• Metaplasia
• Variable Number Tandem Repeat

• Tissue Adhesions
• Fibrosis
• Cystic Fibrosis
• Asthma
• Inflammation
• Dry Eye Syndromes
• Immunologic Deficiency Syndromes

Interacting Proteins

• AMY1A
• HTN1
• PRH1
• STATH

Pathways

• Glycosylation
• Secretion
• Localization
• Pathogenesis
• Transport
• Mucus Secretion
• Cell Differentiation
• Cell Proliferation
• Proteolysis
• Virulence
• Wound Healing
• Epithelial Cell Proliferation
• Biofilm Formation

• Methylation
• Cell Adhesion
• Transposition
• Hypersensitivity
• Protein Secretion
• Oxidative Phosphorylation
• Spermatogenesis

PTMs

• Glycosylation
• Deglycosylation
• Reduction
• Cleavage
• Methylation

• Sulphation
• Phosphorylation
• Acetylation
• Oxidation
• Iodination

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/MUC7

Best Uses Of The MUC7 Marker From Boster Bio

If you're interested in optimizing your experiments using the Boster Bio MUC7 marker, you have a few choices to make when choosing flow procedures. Below are some tips to help you make the best choice for your experiment. If you still have questions, our optimization guides are here to help. They include practical advice to improve the results of your experiments. You can also read our MUC7 Optimization Guide to learn more about this useful marker.

MUC7 is as sensitive as MUC5B

MUC7 is a type of protein that binds to the mucin in the saliva. Although it is not a major component of salivary pellicle, it is a good candidate for antibacterial activity because of its ability to agglutinate bacteria in the mouth. This means that MUC7 is as sensitive as MUC5B in controlling bacterial loads.

The MUC7/SAG-rich samples were more potent in binding S. oralis than MUC5B-rich controls. These samples contained greater relative abundances of Lewis type structures (SLea/x), which include sialic acid and a2,3-linked sialic acid. MUC7/SAG is more abundant than MUC5B, as shown in Figure 1.

Salivary mucins are composed of glycosylated proteins and are produced by the major submandibular, sublingual, and minor mucous glands of the oral cavity. Both MUC5B and MUC7 are highly soluble, and have a range of molecular weights. MUC5B is high-molecular-mass while MUC7 is low-molecular-mass.

In addition to these differences, MUC7 is also more prone to protein contamination. The SDS-PAGE analysis of this MUC7 sample showed that it contains protein contamination. After gel filtration, the sample was further purified using caesium chloride density gradient ultra-centrifugation. This procedure also shows that MUC7 is as sensitive as MUC5B. If you're wondering how to determine if MUC5B is more sensitive than MUC7, consider this study.

MUC7 binding was found to be low in F0392 WT mice, but high in MUC7 WT. The avidity for insoluble mucins was 10-fold lower than for soluble mucins. MUC7 binding was weak in the IE12 WT, and was absent in sample 1 and sample 2. Similarly, MUC7 binding was low in ATCC 10557 WT mice.

MUC2 and MUC5AC cluster on specific chromosomes. They probably derived from a common ancestral gene. MUC5B and MUC7 cluster on chromosome 11p15. Despite the large number of different mucins in mammals, MUC2 and MUC5AC are more prevalent in humans. It has also been reported that MUC5B is dysregulated in mucosal disorders. However, little is known about in vivo regulation of mucin genes. Genetically modified mice have been created to express green fluorescent protein (GFP) sequences. These monomeric GFP sequences were inserted downstream of the last amino acid of gel-forming muc5b.

MUC7 is not a major component of airway mucus. However, genetic association studies suggest that the levels of MUC7 are higher in asthmatic patients. Furthermore, it is thought to have a protective role in lung function and asthma, and its overproduction may be a major cause of chronic airway disease. In addition to MUC5B and MUC7, MUC8 is another poorly characterized putative respiratory mucin.

Transgenic mice are also useful in studying Muc5b production. Transgenic Muc5b-GFP mice are able to measure muc5b production in various tissues of the body, including the vagina. In addition, Muc5b-GFP mice can be used for drug testing in murine models of mucosal diseases. So, in a few years, MUC7 may be as sensitive as MUC5B in the mucosa.

Clinical applications

In the current study, the MUC7 marker was found to be a novel biomarker for Candida neoformans and C. albicans. In this study, we used double labeling to determine whether MUC7 is a direct target of mitochondria or not. We also used a mitochondrion-specific dye, MitoTracker Red CMSRos, as a control to see whether a MUC7 20-mer was detected in the mitochondria of the Candida neoformans fungi.

The MUC7 20-mer peptide was derived from the N-terminus of MUC7 and showed a 53.3% sequence homology to Hsn-5. This peptide is also six times less active against C. albicans than MUC7 51-mer. In addition, it is believed that seven of the eight positively charged amino acids are located within the MUC7 D1 sequence.

The MUC7 20-mer has shown potency against a broad range of bacteria and fungi, and appears to act through a separate mechanism from Hsn-5. This protein is also capable of synergy with other antimicrobial agents found in saliva. This peptide could be a valuable ingredient in the development of artificial saliva formulations. But, it is still unclear whether MUC7 20-mer actually exerts antimicrobial effects in vivo.

While there is no single molecular molecule that makes the MUC7 marker useful, the MUC7 gene can be used to identify specific proteins that cause inflammation and disease. These molecules are also associated with specific chemokines. MUC7 glycosylation may be correlated with the activity of C2GnT and chemokines. This could be a useful biomarker for a multifaceted disease such as asthma.

The MUC7 20-mer and Hsn-5 have similar chemical structures, but different helical structures make them significantly different from each other. In addition, the MUC7 20-mer possesses a stronger amphipathicity. A helical wheel projection of the MUC7 20-mer and Hsn-5 peptide is possible. In addition, a helical wheel projection was made using Genetics Computer Group's sequence analysis software.

The MUC7 peptide has been widely used in the laboratory to diagnose Candida albicans infection. FITC-MUC7 20-mer is a fluorescent peptide that is internalized by C. albicans (DIS) and C. neoformans (CN2). The FITC-MUC7 peptide was observed on the cell membrane of C. albicans, but not in C. albicans.