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AB229880

Anti-GelE antibody

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(1 Publication)

Rabbit Polyclonal GELE antibody. Suitable for WB and reacts with Recombinant full length protein - Enterococcus faecalis samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Enterococcus faecalis V583 gelE aa 150 to C-terminus.

View Alternative Names

EF_1818, gelE, Gelatinase, Coccolysin

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Enterococcus faecalis

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Enterococcus faecalis V583 gelE aa 150 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.

Q833V7

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Enterococcus faecalis": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Recombinant full length protein - Enterococcus faecalis": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/5000", "WB-species-notes": "<p></p>" } } }
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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity >95%.
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

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

GelE also known as gelatinase is a secreted metalloprotease with a mass of approximately 30 kDa. It is produced by certain strains of Enterococcus faecalis a bacterium found in the human gastrointestinal tract and occasionally in other environments such as soil and water. GelE enzymatically degrades gelatin collagen and other proteins therefore contributing to nutrient acquisition. This protease requires zinc as a cofactor for its activity a characteristic feature of metalloproteases.
Biological function summary

The enzymatic activity of GelE involves the breakdown of extracellular matrix components facilitating tissue invasion and colonization. It operates both independently and as part of a complex with other virulence factors. GelE's activity is regulated by a quorum sensing system which controls the expression of genes in response to cell population density. This regulation exemplifies how E. faecalis modulates its pathogenic potential making GelE an important player in bacterial survival and infectivity.

Pathways

GelE plays a critical role in the quorum sensing pathway in Enterococcus faecalis. This pathway involves the fsr locus which encodes a two-component system regulating GelE expression. The pathway includes the fsrA fsrB and fsrC genes and works in conjunction with other proteins like SprE a serine protease. These interactions allow GelE to adapt its function based on environmental cues integrating the protease's activity into the larger bacterial communication network.

GelE contributes to conditions such as endocarditis and urinary tract infections. Its ability to degrade host tissues and immune evasion mechanisms makes it a significant virulence factor in these infections. In such diseases GelE often works alongside other virulence proteins such as Esp an adherence protein enhancing bacterial pathogenicity. Understanding GelE's contribution to pathogenic processes can assist in developing targeted therapies and diagnostic strategies for infections caused by Enterococcus faecalis.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

Metalloprotease capable of the hydrolysis of insoluble hydrophobic substrates. Hydrolyzes azocoll and gelatin and, at a lower rate, soluble and insoluble collagens. Does not cleave short synthetic peptides. Preferentially hydrolyzes the 24-Phe-|-Phe-25 bond in the insulin B-chain, followed by the 5-His-|-Leu-6 bond. Inactivates endothelin-1, primarily by cleavage of the 5-Ser-|-Leu-6 and 16-His-|-Leu-17 bonds. Hydrolyzes the alpha chain of C3 to generate a C3b-like protein. Inhibits complement-mediated hemolysis and opsinization of bacteria. Hydrolyzes the insect antimicrobial peptide cecropin. Decreases the length of E.faecalis chains via the activation of autolysin. Degrades polymerized fibrin.
See full target information gelE
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Publications (1)

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

Immunology 168:63-82 PubMed36240165

2022

Elucidation of the signalling pathways for enhanced exosome release from Mycobacterium-infected macrophages and subsequent induction of differentiation.

Applications

Unspecified application

Species

Unspecified reactive species

Arpana Singh,Kaushik Das,Sampali Banerjee,Prosenjit Sen
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