Recombinant Enterococcus faecalis Gelatinase (gelE) | CSB-EP769310ELW

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CSB-EP769310ELW
Availability:
3 - 7 Working Days
  • Recombinant Enterococcus faecalis Gelatinase (gelE)
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
€352.00 - €1,702.00

Description

Recombinant Enterococcus faecalis Gelatinase (gelE) | CSB-EP769310ELW | Cusabio

Alternative Name(s): Coccolysin

Gene Names: gelE

Research Areas: Others

Organism: Enterococcus faecalis (strain ATCC 700802 / V583)

AA Sequence: VGSEVTLKNSFQVAFNVPVEKSNTGIALHGTDNTGVYHAVVDGKNNYSIIQAPSLVALNQNAVDAYTHGKFVKTYYEDHFQRHSIDDRGMPILSVVDEQHPDAYDNAFWDGKAMRYGETSTPTGKTYASSLDVVGHEMTHGVTEHTAGLEYLGQSGALNESYSDLMGYIISGASNPEIGADTQSVDRKTGIRNLQTPSKHGQPETMAQYDDRARYKGTPYYDQGGVHYNSGIINRIGYTIIQNLGIEKAQTIFYSSLVNYLTPKAQFSDARDAMLAAAKVQYGDEAASVVSAAFNSAGIGAKEDIQVNQPSESVLVNE

Source: E.coli

Tag Info: N-terminal 6xHis-SUMO-tagged

Expression Region: 193-510aa

Sequence Info: Full Length of Mature Protein

MW: 50.5 kDa

Purity: Greater than 90% as determined by SDS-PAGE.

Relevance: 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.

Reference: "Nucleotide sequence of the gelatinase gene (gelE) from Enterococcus faecalis subsp. liquefaciens."Su Y.A., Sulavik M.C., He P., Makinen K.K., Makinen P.L., Fiedler S., Wirth R., Clewell D.B.Infect. Immun. 59:415-420(1991)

Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20?/-80?. The shelf life of lyophilized form is 12 months at -20?/-80?.

Notes: Repeated freezing and thawing is not recommended. Store working aliquots at 4? for up to one week.

Function: 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.

Involvement in disease:

Subcellular Location: Secreted, extracellular space

Protein Families: Peptidase M4 family

Tissue Specificity:

Paythway:

Form: Liquid or Lyophilized powder

Buffer: If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20?/-80?. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Uniprot ID: Q833V7

HGNC Database Link: N/A

UniGene Database Link: N/A

KEGG Database Link: KEGG

STRING Database Link: STRING

OMIM Database Link: N/A

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