Alternative Name(s):

(SVMP)(Hemorrhagic metalloproteinase BaP1)(Bap-1)

Species: (Organism)

Bothrops asper (Terciopelo)

Gene Names:

N/A

Tag info:

N-terminal 10xHis-tagged and C-terminal Myc-tagged

Target Protein AA Sequence:

QQRFSPRYIELAVVADHGIFTKYNSNLNTIRTRVHEMLNTVNGFYRSVDVHAPLANLEVWSKQDLIKVQKDSSKTLKSFGEWRERDLLPRISHDHAQLLTAVVFDGNTIGRAYTGGMCDPRHSVGVVRDHSKNNLWVAVTMAHELGHNLGIHHDTGSCSCGAKSCIMASVLSKVLSYEFSDCSQNQYETYLTNHNPQCILNKP

Expression Region:

192-394aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length of Mature Protein

Pathway:

Mol. Weight:

30.3 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

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.

Research Areas:

Others

Function:

Involvement in disease:

Relevance:

Zinc metalloprotease that exhibits a weak hemorrhagic activity (with a minimum hemorrhagic dose of 20 ug by intradermal and intramuscular injection into mice). The basal membrane components collagen (all chains of type IV) (COL4A4), laminin and nidogen are all degraded by this toxin. Rapidly degrades the Aalpha-chain (FGA) of fibrinogen, and later on, degrades the Bbeta-chain (FGB) of fibrinogen. Also activates the complement system, and induces rat neutrophil chemotaxis. Induces edema in mouse food pad and shows a mild myotoxicity.

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.

Protein Families:

Reference:

"Proteomic analysis of Bothrops pirajai snake venom and characterization of BpirMP, a new P-I metalloproteinase." Bernardes C.P., Menaldo D.L., Camacho E., Rosa J.C., Escalante T., Rucavado A., Lomonte B., Gutierrez J.M., Sampaio S.V. J. Proteomics 80:250-267(2013)