Recombinant Human Mucin 5AC Protein Standard (His tag)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human Mucin 5AC Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.
View Alternative Names
MUC5, MUC5AC, Mucin-5AC, MUC-5AC, Gastric mucin, Major airway glycoprotein, Tracheobronchial mucin, TBM
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Human Mucin 5AC Protein Standard (His tag) (AB316446)
Sandwich ELISA with the capture antibody dilution at 2 ug/mL and detector antibody dilution at 0.5 ug/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Mucin 5AC Protein Standard (His tag) (AB316446)
SDS-PAGE analysis of ab316446 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
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The functions of MUC5AC are central to the maintenance of the protective mucus barrier on epithelial surfaces preventing pathogen invasion and facilitating the clearance of inhaled particles. It is a part of the gel-forming mucin family and often forms complex structures by polymerizing with other mucins like MUC2 and MUC5B contributing to the viscoelastic properties of mucus. These interactions ensure the formation of a stable and robust mucosal barrier.
Pathways
The regulation of MUC5AC production involves several signaling pathways including the EGFR (epidermal growth factor receptor) pathway and the IL-13/STAT6 pathway. These pathways influence mucin production and secretion particularly in response to growth factors and inflammatory cytokines. Proteins such as 13M1 and 11M1 interact with MUC5AC within these pathways modulating its expression and function. This regulation is essential for normal mucus homeostasis and response to environmental challenges.
Specifications
Form
Liquid
General info
Function
Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed : 14535999, PubMed : 14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed : 14535999).
Post-translational modifications
C-, O- and N-glycosylated (PubMed:14718370). O-glycosylated on the second and last Thr of the Thr-/Ser-rich tandem repeats TTPSPVPTTSTTSA (PubMed:14718370, PubMed:22186971, PubMed:25939779). One form of glycosylation is also known as Lewis B (LeB) blood group antigen, a tetrasaccharide consisting of N-acetylglucosamine having a fucosyl residue attached (PubMed:14535999). It has a role as an epitope and antigen and functions as a receptor for H.pylori binding and facilitates infection (PubMed:14535999). C-mannosylation in the Cys-rich subdomains may be required for proper folding of these regions and for export from the endoplasmic reticulum during biosynthesis (PubMed:14718370).. Proteolytic cleavage in the C-terminal is initiated early in the secretory pathway and does not involve a serine protease. The extent of cleavage is increased in the acidic parts of the secretory pathway. Cleavage generates a reactive group which could link the protein to a primary amide.
Target data
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com