protein

Staphylococcus Glu-C

MBS691522

0.25 mg

340 USD

Recombinant Protein

Staphylococcus Glu-C

Glu-C

V8 Protease; Endoproteinase Glu-C

Glutamyl endopeptidase; Glutamyl endopeptidase; Endoproteinase Glu-C; Staphylococcal serine proteinase; V8 protease; V8 proteinase

Glu-C

sspA

SSPA_STAAU

E Coli

Staphylococcus

336

LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLT NKHV VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG D LAIVKFSPN EQNKHIGEVV KPATMSNNAE TQVNQNITVT GYPGDKP VAT MWESKGKITY LKGEAMQYDL STTGGNSGSP VFNEKNEVIG IH WGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNP NN PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA

> 98% by SDS-PAGE & HPLC analysis

Lyophilized

Endotoxin Level: <0.1 ng per ug of protein. Formulation: Lyophilized form 10mM Tris, pH 8.0

Biological Activity: Cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Reconstitution: centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (ex. 0.1% BSA) and store in working aliquots at-20 degree C to -80 degree C. Stability: Lyophilized protein should be stored desiccated below -20 degree C. Upon reconstitution protein should be stored a t4 degree C between 2-7 days and for future use below -20 degree C. Avoid repeated freeze-thaw cycles.

Cytokines & Growth Factors

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at or adjacent to specific residues or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Glu-C cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Recombinant Staphylococcus Glu-C is a 28.8 kDa protease consisting of 266 amino acid residues.

114152163

P0C1U8.1

P0C1U8

28.8 kDa

Function: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases. Ref.3 Ref.4. Catalytic activity: Preferential cleavage: Glu- -Xaa, Asp- -Xaa. Subcellular location: Secreted Ref.3. Post-translational modification: Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA. Miscellaneous: The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through SspA to SspB. Sequence similarities: Belongs to the peptidase S1B family.

0.25 mg

340 USD