Recombinant staphylococcus aureus Glutamyl endopeptidase protein is a Staphylococcus aureus Full Length protein, in the 71 to 336 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC, FuncS.
>95% SDS-PAGE
< 1 EU/µg
Escherichia coli
Tag free
SDS-PAGE, HPLC, FuncS
Yes
L P N N D R H Q I T D T T N G H Y A P V T Y I Q V E A P T G T F I A S G V V V G K D T L L T N K H V V D A T H G D P H A L K A F P S A I N Q D N Y P N G G F T A E Q I T K Y S G E G D L A I V K F S P N E Q N K H I G E V V K P A T M S N N A E T Q V N Q N I T V T G Y P G D K P V A T M W E S K G K I T Y L K G E A M Q Y D L S T T G G N S G S P V F N E K N E V I G I H W G G V P N E F N G A V F I N E N V R N F L K Q N I E D I H F A N D D Q P N N P D N P D N P N N P D N P N N P D E P N N P D N P N N P D N P D N G D N N N S D N P D A A
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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.
Glutamyl endopeptidase
Glutamyl endopeptidase, Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA
Recombinant staphylococcus aureus Glutamyl endopeptidase protein is a Staphylococcus aureus Full Length protein, in the 71 to 336 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC, FuncS.
Glutamyl endopeptidase, Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA
>95% SDS-PAGE
< 1 EU/µg
Escherichia coli
Tag free
SDS-PAGE, HPLC, FuncS
Yes
Active
No
Yes
Staphylococcus aureus
The lyophilized protein is stable at room temperature for up to 1 month. Reconstitute in water to a concentration of 0.1-1.0 mg/ml.
Constituents: 0.121% Tris
L P N N D R H Q I T D T T N G H Y A P V T Y I Q V E A P T G T F I A S G V V V G K D T L L T N K H V V D A T H G D P H A L K A F P S A I N Q D N Y P N G G F T A E Q I T K Y S G E G D L A I V K F S P N E Q N K H I G E V V K P A T M S N N A E T Q V N Q N I T V T G Y P G D K P V A T M W E S K G K I T Y L K G E A M Q Y D L S T T G G N S G S P V F N E K N E V I G I H W G G V P N E F N G A V F I N E N V R N F L K Q N I E D I H F A N D D Q P N N P D N P D N P N N P D N P N N P D E P N N P D N P N N P D N P D N G D N N N S D N P D A A
Full Length
28.8 kDa
71 to 336
Recombinant
Lyophilized
ab98127 is sterile filtered through a 0.2 micron filter. Purity is > 95% by SDS-PAGE gel and HPLC analyses.
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.
Belongs to the peptidase S1B family.
Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of SspA.
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
ab98127 cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Reaction Buffer: 10 mM Tris, pH 8.0
ab98127 cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Reaction Buffer: 10 mM Tris, pH 8.0
This supplementary information is collated from multiple sources and compiled automatically.
Glutamyl endopeptidase also known as GluV8 or GluSE is a serine protease enzyme that is known for its specific cleavage at glutamic acid residues. It has a molecular mass of approximately 27 kDa and is mostly expressed by Staphylococcus aureus. This expression allows the bacteria to modulate host cell functions and defend against host immune responses. The unique ability of glutamyl endopeptidase to target specific peptide bonds distinguishes it from other proteases.
Glutamyl endopeptidase plays a critical role in bacterial pathogenicity. This enzyme does not form part of a larger protein complex but acts independently to degrade host proteins affecting the host cell's integrity. By breaking down structural and immune proteins glutamyl endopeptidase compromises host tissues facilitating bacterial invasion and survival within the host organism. This activity positions it as an important factor in disrupting normal host cellular processes.
Glutamyl endopeptidase is integral to the pathogenicity of Staphylococcus aureus. It participates in the intracellular survival pathway by dismantling host proteins important for immune defense. Additionally its activity influences the cytokine signaling pathway due to its ability to cleave key cytokines and immune regulators. In these pathways it often works alongside other virulence factors like staphopain A collectively promoting bacterial survival and propagation within the host.
Researchers link glutamyl endopeptidase to the development and progression of infections caused by Staphylococcus aureus such as skin abscesses and pneumonia. The enzyme's proteolytic activity contributes to tissue damage and immune evasion making these infections particularly difficult to manage. Glutamyl endopeptidase interacts with host proteins like chemokines influencing inflammatory responses and disease outcome. Understanding its role offers potential therapeutic targets for controlling severe bacterial infections.
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