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About This Item
Nombre del producto
Mucin from bovine submaxillary glands, Type I-S
biological source
bovine submaxillary glands
type
Type I-S
form
powder
composition
Bound sialic acids, 9-24%
technique(s)
electrophoresis: suitable
UniProt accession no.
storage temp.
−20°C
Quality Level
Gene Information
cow ... BSM(286841)
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Application
Mucin from bovine submaxillary glands has been used:
- in the quantification of mucin
- as a component of artificial tear solution
- as a substrate for recombinant sialidase Gardnerella vaginalis
- to investigate a galactose-specific lectin from the red marine alga Ptilota filicina
- to study the characterization of a unique mucin-like glycoprotein secreted by a human endometrial adenocarcinoma cell line (Ishikawa)
Biochem/physiol Actions
Albuminoid substance in mucus which gives it its ropy consistency
Bovine submaxillary mucin (BSM) is thermally stable up to 85°C. The terminal domain regions are key for the adsorption functionality of mucin.
General description
Mucin from bovine submaxillary glands is encoded by two bovine submaxillary BSM genes. It is present in the saliva and interacts with air and food. Mucin comprises three major domains namely N- and C terminal and the glycosylated proline, threonine and serine (PTS domain) central domain. The sialic acid contributes to 30% of the molecular weight of mucin. The central domain has many tandem repeats.
Neuraminidase substrate.
Other Notes
Similar to M 4503, but produced by Sigma.
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A H Sampaio et al.
Phytochemistry, 48(5), 765-769 (1998-07-17)
A lectin from the red marine alga Ptilota filicina (PFL) was isolated by affinity chromatography on cross-linked guar gum. PFL agglutinated native and papain-treated human erythrocytes with preference for type O erythrocytes. The lectin was inhibited by galactose and its
The central domain of bovine submaxillary mucin consists of over 50 tandem repeats of 329 amino acids: Chromosomal localization of the BSM1 gene and relations to ovine and porcine counterparts
Jiang W, et al.
European Journal of Biochemistry, 267(8), 2208-2217 (2000)
Instability and breakup of model tear films
Bhamla MS, et al.
Investigative Ophthalmology & Visual Science, 57(3), 949-958 (2016)
Proteolytic degradation of bovine submaxillary mucin (BSM) and its impact on adsorption and lubrication at a hydrophobic surface
Madsen JB, et al.
Langmuir, 31(30), 8303-8309 (2015)
Hayley Thompson et al.
Journal of bacteriology, 191(11), 3623-3628 (2009-03-24)
Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity. Characterization of a putative sialidase, SiaHI, by others, indicated that this protein alone may not be responsible
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