Recombinant E.Coli Hemolysin E, Chromosomal (HLYE) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-01539P

Greater than 90% as determined by SDS-PAGE.
Recombinant E.Coli Hemolysin E, Chromosomal (HLYE) Protein (His)
Beta LifeScience
SKU/CAT #: BLC-01539P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant E.Coli Hemolysin E, Chromosomal (HLYE) Protein (His) is produced by our E.coli expression system. This is a protein fragment. |
Purity | Greater than 90% as determined by SDS-PAGE. |
Uniprotkb | P77335 |
Target Symbol | HLYE |
Synonyms | hlyE; clyA; hpr; sheA; ycgD; b1182; JW5181; Hemolysin E, chromosomal; Cytotoxin ClyA; Hemolysis-inducing protein; Latent pore-forming 34 kDa hemolysin; Silent hemolysin SheA |
Species | Escherichia coli (strain K12) |
Expression System | E.coli |
Tag | C-6His |
Target Protein Sequence | TEIVADKTVEVVKNAIETADGALDLYNKYLDQVIPWQTFDETIKELSRFKQEYSQAASVLVGDIKTLLMDSQDKYFEATQTVYEWCGVATQLLAAYILLFDEYNEKKASAQKDILIKVLDDGITKLNEAQKSLLVSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDKIRKEAYAGAA |
Expression Range | 2-182aa |
Protein Length | Partial |
Mol. Weight | 21.2 kDa |
Research Area | Others |
Form | Liquid or Lyophilized powder |
Buffer | Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
Reconstitution | Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
Storage | 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Target Details
Target Function | Toxin, which has some hemolytic activity towards mammalian cells. Acts by forming a pore-like structure upon contact with mammalian cells. |
Subcellular Location | Secreted. Periplasm. Host cell membrane; Single-pass membrane protein. Note=Exported from the cell by outer membrane vesicles. Also found in the periplasmic space. |
Protein Families | Hemolysin E family |
Database References | KEGG: ecj:JW5181 |
Gene Functions References
- Membrane-triggered conformational transition of ClyA has been caprured and reported. PMID: 27797514
- The assembly dynamics of the cytolytic pore toxin ClyA has been reported. PMID: 25652783
- These findings show that the clyA+ locus is expressed at an elevated level in the uropathogenic Escherichia coli strain and the authors conclude that this is at least in part due to the effect of the SfaX/PapX transcriptional regulators. PMID: 25178918
- ClyA is delivered to the target host cell in an oligomeric conformation within outer membrane vesicles (OMVs), our findings suggest ClyA forms a prepore oligomeric structure independently of the lipid membrane within the OMV. PMID: 24019520
- Novel site(s) in HlyB responsible for enhancing secretion of cyclodextrin glucanotransferase in E. coli. PMID: 20959127
- in extraintestinal Escherichi coli infections, no HylaA+ sheA+ strains were identified, suggesting possible incompatibility between HlyA and SheA in the chromosome of E. coli PMID: 15956433
- analysis of the hemolysin E (HlyE, ClyA, and SheA) channel in its membrane-bound form PMID: 16754675
- Data Show that hlyE expression in Escherichia coli was controlled by alternate SlyA and H-NS nucleoprotein complexes. PMID: 17892462
- Circular dichroism and fluorescence energy transfer analyses show that HlyE protomers retain an alpha-helical structure when oligomerized to form a pore consisting of parallel HlyE protomers. PMID: 18227266
- results failed to show a positive correlation with SIDS, instead proving that clyA and irp2 genes were common to the infant intestinal E. coli PMID: 19208875