Recombinant Human MUC2 Protein Standard (His tag)
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Recombinant Human MUC2 Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.
View Alternative Names
SMUC, MUC2, Mucin-2, MUC-2, Intestinal mucin-2
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Human MUC2 Protein Standard (His tag) (AB316727)
Sandwich ELISA with the capture antibody dilution at 2 μg/mL and detector antibody dilution at 0.5 μg/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human MUC2 Protein Standard (His tag) (AB316727)
SDS-PAGE analysis of ab316727 under reducing conditions for 2ug protein
Reactivity data
Product details
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
Function
Coats the epithelia of the intestines and other mucus membrane-containing organs to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces (PubMed : 17058067, PubMed : 19432394, PubMed : 33031746). Major constituent of the colon mucus, which is mainly formed by large polymeric networks of MUC2 secreted by goblet cells that cover the exposed surfaces of intestine (PubMed : 19432394, PubMed : 33031746). MUC2 networks form hydrogels that guard the underlying epithelium from pathogens and other hazardous matter entering from the outside world, while permitting nutrient absorption and gas exchange (PubMed : 33031746, PubMed : 36206754). Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (PubMed : 36206754). Binds both Cu(2+) and its reduced form, Cu(1+), at two juxtaposed binding sites : Cu(2+), once reduced to Cu(1+) by vitamin C (ascorbate) or other dietary antioxidants, transits to the other binding site (PubMed : 36206754). MUC2-bound Cu(1+) is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (PubMed : 36206754). Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed : 33031746). Mucin glycoproteins also house and feed the microbiome, lubricate tissue surfaces, and may facilitate the removal of contaminants and waste products from the body (PubMed : 33031746). Goblet cells synthesize two forms of MUC2 mucin that differ in branched chain O-glycosylation and the site of production in the colon : a (1) 'thick' mucus that wraps the microbiota to form fecal pellets is produced in the proximal, ascending colon (By similarity). 'Thick' mucus transits along the descending colon and is lubricated by a (2) 'thin' MUC2 mucus produced in the distal colon which adheres to the 'thick' mucus (By similarity).
Post-translational modifications
O-glycosylated (PubMed:11445551, PubMed:33031746). O-glycosylation is required for mucin assembly (PubMed:33031746). Goblet cells synthesize two forms of mucin that differ in branched chain O-glycosylation and the site of production in the colon (By similarity).. May undergo proteolytic cleavage in the outer mucus layer of the colon, contributing to the expanded volume and loose nature of this layer which allows for bacterial colonization in contrast to the inner mucus layer which is dense and devoid of bacteria.. At low pH of 6 and under, undergoes autocatalytic cleavage in vitro in the N-terminal region of the fourth VWD domain. It is likely that this also occurs in vivo and is triggered by the low pH of the late secretory pathway.
Target data
Product promise
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