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AB238238

Recombinant kgp protein (Tagged)

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(1 Publication)

Recombinant kgp protein (Tagged) is a Porphyromonas gingivalis ATCC 33277 Fragment protein, in the 229 to 594 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

PGN_1728, kgp, Lys-gingipain, Lysine-specific cysteine proteinase Kgp

3 Images
Mass Spectrometry - Recombinant kgp protein (Tagged) (AB238238)
  • Mass Spec

Supplier Data

Mass Spectrometry - Recombinant kgp protein (Tagged) (AB238238)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab238238 could indicate that this peptide derived from E.coli-expressed Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257) kgp.

Mass Spectrometry - Recombinant kgp protein (Tagged) (AB238238)
  • Mass Spec

Unknown

Mass Spectrometry - Recombinant kgp protein (Tagged) (AB238238)

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of ab238238 could indicate that this peptide derived from E.coli-expressed Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257) kgp.

SDS-PAGE - Recombinant kgp protein (Tagged) (AB238238)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant kgp protein (Tagged) (AB238238)

(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) analysis with 5% enrichment gel and 15% separation gel of ab238238.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

B2RLK2

Animal free

No

Carrier free

No

Species

Porphyromonas gingivalis ATCC 33277

Storage buffer

pH: 7.2 - 7.4 Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"DVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEAEVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKVTDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYLEKALLIAGADSYWNPKIGQQTIKYAVQYYYNQDHGYTDVYSYPKAPYTGCYSHLNTGVGFANYTAHGSETSWADPSLTATQVKALTNKDKYFLAIGNCCVTAQFDYPQPCFGEVMTRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFGVQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGAHYYWEAYHVLGDGSVM","proteinLength":"Fragment","predictedMolecularWeight":"56.6 kDa","actualMolecularWeight":null,"aminoAcidEnd":594,"aminoAcidStart":229,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"B2RLK2","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Kgp also known as lysine gingipain is a bacterially derived cysteine protease. This enzyme has an approximate mass of 50 kDa and exhibits its activity primarily in the bacterium Porphyromonas gingivalis. Kgp is found mainly in the outer membrane vesicles and is secreted in the extracellular environment of this bacterium. It is characterized by its specificity for peptide bonds at lysine residues which differentiates it from its counterpart arginine gingipain.
Biological function summary

Lysine gingipain contributes to the pathogenicity of Porphyromonas gingivalis by degrading host proteins and evading immune responses. It is an important component of the protein complex associated with the bacterium's ability to colonize and persist in the host's tissues. Kgp activity modulates interactions with the host facilitating bacterial adherence and invasion into tissues. Consequently it plays a significant role in the bacterium's capability to sustain infection and cause damage to the host's immune system.

Pathways

The involvement of lysine gingipain is important in pathways related to inflammatory response and immune evasion. The enzyme interacts with complement proteins and influences the kallikrein-kinin system. Additionally it relates functionally with proteins like gingipain R both involved in processing extracellular matrix components which furthers the pathogenic mechanisms of Porphyromonas gingivalis. This protease's activity influences critical host-pathogen interactions that drive inflammation and tissue destruction.

Lysine gingipain connects strongly with periodontitis and cardiovascular disease. Its enzymatic actions lead to the degradation of periodontal structures in periodontitis. Kgp can enter the bloodstream where it may modulate the immune system potentially affecting cardiovascular health. The protease interacts with proteins involved in these diseases such as gingipain R boosting inflammatory damage and contributing to systemic manifestations beyond oral health.

Specifications

Form

Liquid

General info

Function

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.

Sequence similarities

Belongs to the peptidase C25 family.

Post-translational modifications

Proteolytically cleaved into a catalytic subunit and three adhesins. Arg-gingipain is involved in this post-translational processing (By similarity).

Product protocols

Target data

Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria.
See full target information kgp

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Oxidative medicine and cellular longevity 2022:5265616 PubMed36035217

2022

Contribution of Adiponectin/Carnitine Palmityl Transferase 1A-Mediated Fatty Acid Metabolism during the Development of Idiopathic Pulmonary Fibrosis.

Applications

Unspecified application

Species

Unspecified reactive species

Wenjuan Wu,Guojun Zhang,Lingxiao Qiu,Xueya Liu,Shuai Zhou,Jizhen Wu
View all publications

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