Staphylococcus aureus Glutamyl endopeptidase
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| Amount : | 500 µg |
| Purification : | Reducing and Non-Reducing SDS PAGE at >= 95% |
| Content : | Lyophilized from a sterile (0.2 micron) filtered aqueous solution containing 10 mM sodium phosphate, pH 7.5 Sterile water at 0.1 mg/mL |
| Storage condition : | Store at -20°C |
| AA sequence : | MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA |
| Gene : | sspA |
| Uniprot ID : | P0C1U8 |
| Alternative Name : | Glutamyl endopeptidase, Endoproteinase Glu-C, Staphylococcal serine proteinase,V8 protease, V8 proteinase            |
Source: Genetically modified E.coli.
Predicted MW: Monomer, 28.9 kDa (267 aa)
Glutamyl endopeptidase (Glu-C) is an enzyme from Staphylococcus aureus strain V8 that hydrolizes peptide bonds formed on the carboxyl terminal side of aspartate and glutamate amino acid residues. Glu-C is pathogenic to human tissue and functions during adherence and colonization of host cells. Glu-C protects against host defense mechanisms by fragmenting human immunoglobulins IgG, IgM, and IgA.
Endotoxin: Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Centrifuge vial before opening, Suspend the product by gently pipetting the above recommended solution down the sides of the vial. DO NOT VORTEX. Allow several minutes for complete reconstitution. For prolonged storage, dilute to working aliquots in a 0.1% BSA solution, store at -80°C and avoid repeat freeze thaws. Upon reconstitution, a small amount of visible precipitate can be expected. A 10% overfill has been added to the total material vialed to compensate for this loss.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Secreted |
| Post transnational modification: | Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA. |
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