Recombinant Viridovipera stejnegeri Snake venom serine protease 5

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Description

Background on Serine Proteases in Snake Venom

Serine proteases in snake venom are known for their diverse biological activities, including fibrinogenolysis, plasminogen activation, and clot dissolution . These enzymes are highly variable, with different species exhibiting unique proteases that target various stages of the blood coagulation cascade. For example, Trimeresurus stejnegeri (now known as Viridovipera stejnegeri) venom contains several fibrinogenolytic enzymes like stejnefibrase-1, -2, and -3, which degrade fibrinogen and prevent clot formation .

Potential Applications and Research Findings

While specific data on "Recombinant Viridovipera stejnegeri Snake venom serine protease 5" is not available, recombinant serine proteases in general offer potential therapeutic applications. They can be used to develop novel treatments for blood coagulation disorders and snakebite envenoming . The study of these enzymes also provides insights into the evolution and diversity of snake venom components, aiding in the development of more effective antivenoms .

Data Tables and Comparative Analysis

Given the lack of specific data on "Recombinant Viridovipera stejnegeri Snake venom serine protease 5," we can compare the characteristics of serine proteases from related species:

EnzymeMolecular Weight (kDa)FunctionSource
Stejnefibrase-150FibrinogenolysisViridovipera stejnegeri
Stejnefibrase-231Fibrinogenolysis (Bβ-chain)Viridovipera stejnegeri
Stejnefibrase-332Fibrinogenolysis (Aα & Bβ-chains)Viridovipera stejnegeri
Rhinocerase36 (native), 31 (deglycosylated)Fibrinogenolysis, clot dissolutionBitis gabonica rhinoceros

Product Specs

Form
Lyophilized powder
Note: While we prioritize shipping the format currently in stock, please specify your preferred format in order notes for customized preparation.
Lead Time
Delivery times vary depending on the purchasing method and location. Please consult your local distributor for precise delivery estimates.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
Notes
Avoid repeated freeze-thaw cycles. Store working aliquots at 4°C for up to one week.
Reconstitution
Centrifuge the vial briefly before opening to collect the contents. Reconstitute the protein in sterile deionized water to a concentration of 0.1-1.0 mg/mL. For long-term storage, we recommend adding 5-50% glycerol (final concentration) and aliquoting at -20°C/-80°C. Our standard glycerol concentration is 50% and can be used as a reference.
Shelf Life
Shelf life depends on several factors, including storage conditions, buffer composition, temperature, and protein stability. Generally, liquid formulations have a 6-month shelf life at -20°C/-80°C, while lyophilized forms have a 12-month shelf life at -20°C/-80°C.
Storage Condition
Upon receipt, store at -20°C/-80°C. Aliquoting is recommended for multiple uses. Avoid repeated freeze-thaw cycles.
Tag Info
Tag type is determined during manufacturing.
The tag type is determined during production. Please specify your required tag type for preferential development.
Synonyms
; Snake venom serine protease 5; SVSP; EC 3.4.21.-
Buffer Before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Datasheet
Please contact us to get it.
Expression Region
25-258
Protein Length
Full Length of Mature Protein
Purity
>85% (SDS-PAGE)
Species
Trimeresurus stejnegeri (Chinese green tree viper) (Viridovipera stejnegeri)
Target Protein Sequence
VVGGRP CNINEHRSLV VLFNSSGFLC GGTLINQDWV VTAAHCDSNN FQMIFGVHSK NVPNEDEQRR VPKEKFFCDS NKNYTQWNKD IMLIRLNSPV NNSTHIAPLS LPSSPPIVGS VCRIMGWGTI TFPNETYPDV PHCANINLFN YTVCHGAHAG LPATSRTLCA GVLEGGKDTC KGDSGGPLIC NGQFQGIVSW GGHPCAQPRE PGVYTKVFDH LDWIQNIIAG NTTATCPL
Uniprot No.

Target Background

Function
Snake venom serine protease potentially involved in the prey's hemostasis system.
Protein Families
Peptidase S1 family, Snake venom subfamily
Subcellular Location
Secreted.
Tissue Specificity
Expressed by the venom gland.

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