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M3895

Sigma-Aldrich

Mucin from bovine submaxillary glands

Type I-S

Synonym(s):

MUC

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About This Item

CAS Number:
84195-52-8
EC Number:
282-357-4
MDL number:
MFCD00131629
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine submaxillary glands

Quality Level

200

type

Type I-S

form

powder

composition

Bound sialic acids, 9-24%

technique(s)

electrophoresis: suitable

UniProt accession no.

P98091

storage temp.

−20°C

Gene Information

cow ... BSM(286841)

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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.

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

Bovine submaxillary mucin (BSM) is thermally stable up to 85°C. The terminal domain regions are key for the adsorption functionality of mucin.
Albuminoid substance in mucus which gives it its ropy consistency

Linkage

Similar to M 4503, but produced by Sigma.

Substrates

Neuraminidase substrate.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Identification and characterization of NanH2 and NanH3, enzymes responsible for sialidase activity in the vaginal bacterium Gardnerella vaginalis
Robinson LS, et al.
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