Recombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1, Bothrops atrox (Barba amarilla) (Fer-de-lance), E.coli, N-terminal 10xHis-tagged and C-terminal Myc-tagged, 30.4kDa, purity >85% as determined by SDS-PAGE.

Recombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1

Recombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1 — Snake venom zinc metalloproteinase, which causes strong hemorrhagy and dermonecrosis by degrading the extracellular matrix. Purity >85%.

SKU: BCRECP-003554 Category:
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Product Specifications

Product SkuBCRECP-003554
Product DescriptionRecombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1 Protein is expressed from E.coli with N-terminal 10xHis-tagged and C-terminal Myc-tagged. It contains 1-202aa. [Accession | P85420].
Uniprot No.P85420
PurityGreater than 85% as determined by SDS-PAGE.
Expression SystemE.coli
Expression Region1-202aa
SpeciesBothrops atrox (Barba amarilla) (Fer-de-lance)
Tag InfoN-terminal 10xHis-tagged and C-terminal Myc-tagged
Molecular weight30.4kDa
ActivityPlease contact us to obtain bioactivity data.
BufferIf 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.
StorageStore at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Research AreasOthers

Function

Snake venom zinc metalloproteinase, which causes strong hemorrhagy and dermonecrosis by degrading the extracellular matrix. Its strong hemorrhagic activity is independent of binding to extracellular matrix (ECM) proteins and is instead due to its high catalytic activity, in contrast to P-III metalloproteinases, which bind to the ECM but have lower catalytic activity. Its unique dermonecrotic action may be explained by its efficacy in laminin hydrolysis (Probable).

Biological Context

Subcellular Location: Secreted
Tissue Specificity: Expressed by the venom gland

Product Specifications

Recombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1 is a recombinant protein from Bothrops atrox (Barba amarilla) (Fer-de-lance), expressed in E.coli, covering amino acids 1-202aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 30.4kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.

Recommended applications depend on the target, product format, and product-specific validation data. Refer to the product datasheet or Certificate of Analysis (CoA), or contact BioCrest Sci for application guidance.

Biological Activity: Please contact us to obtain bioactivity data.

Storage: Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shipping & Lead Time: Availability, shipping conditions, and estimated lead time are confirmed in the formal quotation or order confirmation based on the product format, destination, and order requirements.

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Protein Biology

Function

Snake venom zinc metalloproteinase, which causes strong hemorrhagy and dermonecrosis by degrading the extracellular matrix (PubMed:20102699, PubMed:28767072). Its strong hemorrhagic activity is independent of binding to extracellular matrix (ECM) proteins and is instead due to its high catalytic activity, in contrast to P-III metalloproteinases, which bind to the ECM but have lower catalytic activity (PubMed:28767072). Its unique dermonecrotic action may be explained by its efficacy in laminin hydrolysis (Probable). Cleaves Xaa-Leu bonds (PubMed:20102699). Hydrolyzes fibrinogen, fibrin, fibronectin (FN1), type I collagen, type IV collagen, laminin, nidogen, integrin alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1) (PubMed:20102699, PubMed:28767072). Binds to fibronectin (FN1) and fibrinogen (PubMed:20102699). Shows no or very weak binding to type I collagen and laminin, and no binding to type IV collagen and nidogen (PubMed:20102699, PubMed:28767072). Inhibits ADP- and collagen-induced platelet aggregation both in the presence (IC(50)=1.4 uM for collagen) and in the absence (IC(50)=2.2 uM for collagen) of cofactors (PubMed:20102699)

Subcellular Location

Secreted

Tissue Specificity

Expressed by the venom gland

Subunit

Monomer

Organism: Bothrops atrox  |  Synonyms: Atroxlysin-Ia; BATXSVMPI5

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Availability, dispatch timing, shipping conditions, and delivery estimates depend on the product format, destination, and order requirements. These details are confirmed in the formal quotation or order confirmation.

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Quality-control data such as identity, purity, endotoxin level, or biological activity are provided only when specified on this product page, the datasheet, or Certificate of Analysis (CoA). Biological activity is not implied unless explicitly stated.

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