Recombinant Bothrops asper Snake venom metalloproteinase BaP1

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Cat. No.

BT38270

Source

Yeast

Synonyms

Snake venom metalloproteinase BaP1; SVMP; EC 3.4.24.-; Hemorrhagic metalloproteinase BaP1; Bap-1

Purity

>85% (SDS-PAGE)

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Cat. No.

BT38270

Source

E.coli

Synonyms

Snake venom metalloproteinase BaP1; SVMP; EC 3.4.24.-; Hemorrhagic metalloproteinase BaP1; Bap-1

Purity

>85% (SDS-PAGE)

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Cat. No.

BT38270

Source

Baculovirus

Synonyms

Snake venom metalloproteinase BaP1; SVMP; EC 3.4.24.-; Hemorrhagic metalloproteinase BaP1; Bap-1

Purity

>85% (SDS-PAGE)

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Cat. No.

BT38270

Source

Mammalian cell

Synonyms

Snake venom metalloproteinase BaP1; SVMP; EC 3.4.24.-; Hemorrhagic metalloproteinase BaP1; Bap-1

Purity

>85% (SDS-PAGE)

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Description

Introduction

BaP1 is a 22.7-kDa P-I class snake venom metalloproteinase (SVMP) isolated from Bothrops asper venom, a medically significant species in Central America. It induces severe tissue damage, including hemorrhage, myonecrosis, and inflammation, through proteolytic activity and cytokine modulation . To address the limitations of traditional antivenom production (e.g., batch variability, animal immunization), recombinant antibody technologies have been developed to neutralize BaP1. This article focuses on the recombinant single-chain variable fragment (scFvBaP1) engineered against BaP1, its structural and functional properties, and its therapeutic potential.

Structure and Biochemical Properties

BaP1 (Native)

Molecular Weight: 22.7 kDa .
Active Site: Zinc-dependent, with a consensus sequence H142E143XXH146XXGXXH152 and a Met-turn motif (C164I165M166) .
Disulfide Bridges: Three bridges (Cys117-Cys197, Cys159-Cys181, Cys157-Cys164) stabilize the structure .
Subdomains: Major (residues 1–152) and minor (residues 153–202) domains linked by a shallow active-site cleft .

Recombinant scFvBaP1

Format: Single-chain variable fragment (VH-VL linked by a (G4S)3 peptide) fused to a SUMO tag (13.6 kDa) .
Molecular Weight: ~43 kDa (SUMO + scFv) .
Expression: Expressed in E. coli C43(DE3) as a cytoplasmic protein .

Neutralization Efficacy

Activity	Neutralization by scFvBaP1	Mechanism
Fibrinolysis	50% inhibition at 1.25 µM	Direct binding to BaP1’s active site, disrupting proteolytic activity .
Hemorrhage	Complete neutralization	Blocks BaP1-mediated endothelial damage and cytokine release .
Muscle Necrosis	Complete neutralization	Inhibits myotoxic effects via antibody-mediated toxin sequestration .
Inflammation	Reduced cytokine release	Suppresses IL-1, TNF-α, and IL-6 production triggered by BaP1 .

Therapeutic Implications

Advantages Over Traditional Antivenoms:
- Consistent batch quality through recombinant production .
- Reduced immunogenicity compared to horse-derived antivenoms .
- Targeted neutralization of BaP1, a key pathogenic component .
Future Directions:
- Combination therapies with inhibitors of SVMP-induced cytokine cascades .
- Engineering scFvBaP1 for improved pharmacokinetics (e.g., half-life extension) .

Research Findings

Study	Key Discovery
Docking Analyses	Predicted binding modes of scFvBaP1 to BaP1’s active site .
In Vivo Studies	scFvBaP1 neutralizes BaP1-induced tissue damage in animal models .
Structural Biology	Crystallographic confirmation of BaP1’s zinc-binding motif .
Immunological Studies	BaP1 activates complement system and cytokine networks, exacerbating inflammation .

Product Specs

Form

Lyophilized powder. We will preferentially ship the available format. For specific format requirements, please note them when ordering.

Lead Time

Delivery times vary by purchasing method and location. Consult local distributors for specific delivery times. Proteins are shipped with blue ice packs by default. Request dry ice shipment in advance (extra fees apply).

Notes

Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.

Reconstitution

Briefly centrifuge the vial before opening. Reconstitute protein in sterile deionized water to 0.1-1.0 mg/mL. Add 5-50% glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final glycerol concentration is 50%.

Shelf Life

Shelf life depends on storage conditions, buffer, temperature, and protein stability. Liquid form: 6 months at -20°C/-80°C. Lyophilized form: 12 months at -20°C/-80°C.

Storage Condition

Store at -20°C/-80°C upon receipt. Aliquot for multiple uses. Avoid repeated freeze-thaw cycles.

Tag Info

Tag type is determined during manufacturing. If you have a specific tag type requirement, please inform us for preferential development.

Synonyms

Snake venom metalloproteinase BaP1; SVMP; EC 3.4.24.-; Hemorrhagic metalloproteinase BaP1; Bap-1

Buffer Before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Datasheet

Please contact us to get it.

Expression Region

192-394

Protein Length

Full Length of Mature Protein

Purity

>85% (SDS-PAGE)

Species

Bothrops asper (Terciopelo)

Target Protein Sequence

QQRFSPRYI ELAVVADHGI FTKYNSNLNT IRTRVHEMLN TVNGFYRSVD VHAPLANLEV WSKQDLIKVQ KDSSKTLKSF GEWRERDLLP RISHDHAQLL TAVVFDGNTI GRAYTGGMCD PRHSVGVVRD HSKNNLWVAV TMAHELGHNL GIHHDTGSCS CGAKSCIMAS VLSKVLSYEF SDCSQNQYET YLTNHNPQCI LNKP

Uniprot No.

P83512

Target Background

Function

Zinc metalloprotease with weak hemorrhagic activity (minimum hemorrhagic dose: 20 µg via intradermal/intramuscular injection in mice). Degrades basement membrane components: collagen IV (all chains), laminin, and nidogen. Rapidly degrades fibrinogen's Aα-chain (FGA), then the Bβ-chain (FGB). Activates the complement system and induces rat neutrophil chemotaxis. Induces edema in mouse footpad and mild myotoxicity.

Protein Families

Venom metalloproteinase (M12B) family, P-I subfamily

Subcellular Location

Secreted.

Tissue Specificity

Expressed by the venom gland.

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Recombinant Bothrops asper Snake venom metalloproteinase BaP1

Description

Introduction

Structure and Biochemical Properties

BaP1 (Native)

Recombinant scFvBaP1

Neutralization Efficacy

Therapeutic Implications

Research Findings

Product Specs

Target Background

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