GeneBio Systems
Recombinant Staphylococcus aureus DNA-binding protein HU (hup)
Recombinant Staphylococcus aureus DNA-binding protein HU (hup)
SKU:Q5HFV0
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Size: 100ug. Other sizes are also available.
Activity: Not tested
Research Areas: Others
Uniprot ID: Q5HFV0
Gene Names: hup
Alternative Name(s):
Abbreviation: Recombinant Staphylococcus aureus hup protein
Organism: Staphylococcus aureus (strain COL)
Source: E.coli
Expression Region: 1-90aa
Protein Length: Full Length
Tag Info: C-terminal 6xHis-tagged
Target Protein Sequence: MNKTDLINAVAEQADLTKKEAGSAVDAVFESIQNSLAKGEKVQLIGFGNFEVRERAARKGRNPQTGKEIDIPASKVPAFKAGKALKDAVK
MW: 16.5 kDa
Purity: Greater than 90% as determined by SDS-PAGE.
Endotoxin: Not test
Biological_Activity:
Form: Liquid or Lyophilized powder
Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Relevance: Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. The minor subunit is the nucleation component of curlin monomers. Coexpression of cellulose and thin aggregative fimbriae (curli fimbrae or fibers) leads to a hydrophobic network with tightly packed cells embedded in a highly inert matrix that confers cohesion, elasticity and tissue-like properties to colonies
Reference: "Cellulose as an architectural element in spatially structured Escherichia coli biofilms." Serra D.O., Richter A.M., Hengge R. J. Bacteriol. 195: 5540-5554(2013)
Function:
