Recombinant Mucin 5AC Monoclonal Antibody (AN301037L)
For research use only.
| Verified Samples |
Verified Samples in WB: HT-29 Verified Samples in IHC: Human stomach tissue, Rat stomach tissue |
| Dilution | IHC 1:200-1:1000, WB 1:1000-1:5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Mucin 5AC protein |
| Abbre | Mucin 5AC |
| Synonyms | gastric mucin|mucin, MUC, MUC5AC, MUC5, TBM, leB, mucin, mucin-5AC, MUC5A, Apomucin, Gastric mucin, gastric mucin|mucin 5, Major airway glycoprotein, MUC 5, Mucin 5 Subtypes A And C, Mucin 5AC, Mucin-5 subtype AC, subtypes A and C, tracheobronchial, tracheobronchial/gastric|mucin 5AC|tracheobronchial mucin, MUC-5AC, Mucin 5 Subtype AC, Tracheobronchial mucin, Apomucin Major Airway Glycoprotein, Lewis B blood group antigen, Mucin 5, Mucin 5 subtype AC tracheobronchial, Mucin 5 subtypes A and C tracheobronchial/gastric, Mucin 5AC oligomeric mucus/gel forming, oligomeric mucus/gel forming pseudogene, Tracheobronchial Mucin (TBM), tracheobronchial/gastric, MUC5AC |
| Swissprot | |
| Calculated MW | 586 kDa |
| Observed MW |
586 kDa
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Cytoplasm |
| Tissue Specificity | Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum. |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction, Cancer |
| Clone No. | 6C4 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | The cysteine residues in the Cys-rich subdomain repeats are not involved in disulfide bonding.,Gel-forming glycoprotein of gastric and respiratoy tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microrganisms and particules that are subsequently removed by the mucocilary system.,PTM:C-, O- and N-glycosylated. O-glycosylated on the Thr-/Ser-rich tandem repeats. 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.,PTM: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.,similarity:Contains 1 CTCK (C-terminal cystine knot-like) domain.,similarity:Contains 2 VWFC domains.,similarity:Contains 4 VWFD domains.,subunit:Multimeric. Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD).,tissue specificity:Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.：{{item.cat}}
{{index}} {{goods_show_value}}
-
IF：{{item.impact}}
Journal：{{item.journal}} ({{item.year}})
DOI：{{item.doi}}Reactivity：{{item.species}}
Sample Type：{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
