Comparison

Recombinant Enterococcus faecalis Gelatinase(gelE)

Item no. CSB-EP769310ELW-10
Manufacturer Cusabio
Amount 10 ug
Quantity options 1 mg 10 ug 100 ug 20 ug 200 ug 50 ug 500 ug
Category
Type Proteins Recombinant
Format Liquid or Lyophilized powder
Specific against other
Host E.coli
Conjugate/Tag SUMO, HIS
Purity Greater than 90% as determined by SDS-PAGE.
Sequence VGSEVTLKNSFQVAFNVPVEKSNTGIALHGTDNTG VYHAVVDGKNNYSIIQAPSLVALNQNAVDAYTHGK FVKTYYEDHFQRHSIDDRGMPILSVVDEQHPDAYD NAFWDGKAMRYGETSTPTGKTYASSLDVVGHEMTH GVTEHTAGLEYLGQSGALNESYSDLMGYIISGASN PEIGADTQSVDRKTGIRNLQTPSKHGQPETMAQYD DRARYKGTPYYDQGGVHYNSGIINRIGYTIIQNLG IEK
Protein Family Peptidase M4 family
Citations "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)
ECLASS 10.1 32160409
ECLASS 11.0 32160409
UNSPSC 12352202
Alias Coccolysin
Available
Manufacturer - Targets
gelE
Manufacturer - Conjugate / Tag
N-terminal 6xHis-SUMO-tagged
Storage Conditions
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 -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.
Molecular Weight
50.5 kDa
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.
Expression Region
193-510aa
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4C 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.
Subcellular Location
Secreted, extracellular space
Biologically active
Not Test
Protein length
Full Length of Mature Protein

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 10 ug
Available: In stock
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