Creative Biolabs is offering the most comprehensive services for antibody development projects. With strict regulation and effective execution, we are dedicated to providing the most valuable solutions to complete your projects.
HighlightsWith over a decade of experience in phage display technology, Creative Biolabs can provide a series of antibody or peptide libraries that are available for licensing or direct screening. These ready-to-use libraries are invaluable resources for isolating target-specific binders for various research, diagnostic or therapeutic applications. Highlights
Creative Biolabs has established a broad range of platforms for developing novel antibodies or equivalents. These cutting-edge technologies enable our scientists to meet your demands from different aspects and tailor the most appropriate solution that contributes to the success of your projects.
HighlightsWith deep understanding in antibody-related realms and extensive project experience, Creative Biolabs offers a variety of references to help you learn more about our capacities and achievements, including infographic, flyer, case study, peer-reviewed publications, and all kinds of knowledge that can assist your projects. You are also welcome to contact us directly for more specific solutions.
HighlightsGet a real taste of Creative Biolabs, one of the most professional custom service providers in the world. We are committed to providing highly customized comprehensive solutions with the best quality to advance your projects.
HighlightsSLC50A1 (solute carrier family 50, member 1), also known as sugar transporter SWEET1 or stromal cell protein (SCP), is a Na+-independent anion exchanger (AE). It belongs to the Slc4a family of Cl-/HCO3- exchangers that contain products of 11 human genes (SLC4A1-5; A6, A7-11). They are composed of Na+-independent anion exchangers (AEs) SLC4A1 (AE1), SLC4A2 (AE2), SLC4A3 (AE3), and SLC50A1 (AE4) and Na+-coupled bicarbonate transporters (NBCs). There are structural and functional similarities between all transporters of the SLC4 gene family. AE polypeptides consist of three distinct domains: a hydrophilic cytoplasmic N-terminal domain of ~400-700 amino acids, a hydrophobic transmembrane domain of ~500 amino acids, and a cytoplasmic C-terminal consisting of ~30-100 amino acids.
| Basic Information of SLC50A1 | |
| Protein Name | Sugar transporter SWEET1 |
| Gene Name | SLC50A1 |
| Aliases | RAG1AP1, SCP |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q9BRV3 |
| Transmembrane Times | 7 |
| Length (aa) | 221 |
| Sequence | MEAGGFLDSLIYGACVVFTLGMFSAGLSDLRHMRMTRSVDNVQFLPFLTTEVNNLGWLSYGALKGDGILIVVNTVGAALQTLYILAYLHYCPRKRVVLLQTATLLGVLLLGYGYFWLLVPNPEARLQQLGLFCSVFTISMYLSPLADLAKVIQTKSTQCLSYPLTIATLLTSASWCLYGFRLRDPYIMVSNFPGIVTSFIRFWLFWKYPQEQDRNYWLLQT |
SLC50A1 (AE4) is a membrane protein involved in anion exchange. It has been found to be expressed on the apical membrane of gastric mucous cells and duodenal epithelial cells in mouse, rabbit, and human. However, the function of AE4 in HCO3- secretion and chloride absorption in gastric and duodenal epithelial cells is not clear. Early research found that AE4 is a Na+-independent anion exchanger. However, a recent study revealed that it is an electroneutral monovalent cation-dependent Cl-/HCO3- exchanger that mediates Cl-/HCO3- exchange activity in the presence of K+ as well as Cs+, Li+, and Rb+. SLC4 family members have been shown to play an important role in exocrine gland fluid secretion by promoting intracellular Cl- accumulation. Indeed. the expression of AE4 is found in secretory acinar cells such as salivary gland acinar cells and involved in the regulation of intracellular Cl- accumulation in exchange for KHCO3- efflux. Mice lacking AE4 Cl-/HCO3- exchangers will reduce HCO3--dependent Cl- uptake and thus decrease saliva secretion. These suggest AE4 appears to play an important role in fluid secretion.
Fig.1 Na+-dependent HCO3-/HCO3- exchange under low Cl- concentrations. (Peña-Münzenmayer, 2016)
The study identifies SLC50A1 as an electroneutral Cl(-)/nonselective cation-HCO3(-) exchanger and demonstrates AE4 promotes Cl(-) influx in exchange for K(+)(Na(+)) and HCO3(-) ions in secretory cells.
The research makes a conclusion that AE4 is functionally expressed in submandibular acinar cells and involved in the cAMP-dependent regulation of fluid secretion.
In this study, a mathematical model of a salivary gland acinar cell is used to investigate the role of Ae2 (Slc4a2) and Ae4 (SLC50A1) in saliva secretion and the results show that Ae4 plays an important role in saliva secretion.
The aim of this study is to investigate the three-dimensional (3-D) expression and distribution of SLC26A4 and AE4 in β-intercalated cells (β-ICs) of the rabbit cortical collecting duct. And the results show that acidosis reduces AE4 expression in β-ICs and diminishes pendrin in apical recycling endosomes.
The article demonstrates that AE4 promoter appears to be a direct target of forkhead transcription factor Foxi1.
Based on the versatile Magic™ membrane protein production platform, Creative Biolabs can help you to obtain the best soluble and functional target protein to make your project a success. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC50A1 antibody development services.
As a forward-looking biotech company as well as a leading custom service provider in the field of membrane protein, Creative Biolabs has won a good reputation among our worldwide customers for successfully accomplishing numerous challenging projects including generation of many functional membrane proteins. Please feel free to contact us for more information.
Reference
All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.
