Cobra Venom Factor, Recombinant

Sustainable, animal friendly and scalable

HC4073 is the scalable recombinant form of Cobra venom factor (CVF). Native CVF will be increasingly difficult to obtain. The rCVF is an indefinite and available source with strong reduced local restrictions or regulations.

Quantity:
50 µg
Catalog #:
HC4073

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HC4073 is the recombinant form of Cobra venom factor (CVF). The complement system is the first line of defense against pathogens and important component of innate as well as adaptive immunity. CVF is the non-toxic complement activating protein in the venom from the cobra species Naja Kaouthia.

CVF is a structural and functional analog of complement C3. The protein functionally resembles C3b and exhibits a three-chain structure like C3c. CVF forms a C3/C5 convertase with factor B in the presence of factor D and Mg2+, thereby activating the alternative pathway of complement. Although analog in function, there are two differences between CVF Bb convertases and natural C3bBb convertases.

- First the stability is quite different. Whereas C3bBb is short-lived with a half-life of 1.5 min, CVF Bb is rather stable with a half-life of 7h.

- Secondly, factor H disassembles C3bBb and serves as cofactor for proteolytic inactivation of C3b by factor I. The CVF convertase is completely resistant to factor H and I. Which makes it an excellent research tool.

CVF is widely used reagent in order to deplete serum samples in order to study the role of complement in host defense, immune response and pathogenesis of disease. Since the Naja species are on the list of endangered species, native CVF will increasingly difficult to obtain.

The recombinant protein (rCVF) is synthesized in insect cells and is processed into a two-chain form of pro-CSF that structurally resembles C3 (Vogel et al). Pro-CVF can present in three forms and have all functional activity of mature, native CVF.

The activity of pro-CVF and the resulting convertase is indistinguishable from CVF and the C3bBb convertase. rCVF can be exploited in vitro as well as in animals. This leads to decomplemented serum and high concentration of complement end products, like C3a, C5a and sTCC.

The key advantages:

 - Indefinite source

 - Easy im- and export

 - Scalable recombinant

 - Sustainable and animal friendly

Documents:

> Read and meet our complement research functional tools

Specifications
Product type Proteins
Quantity 50 µg
Alias CVF, CVFk
Formulation 50 µg (100 µg/ml) in PBS
Application Functional studies, Western blot
Storage and stability Product should be stored at -80°C. Store stock solution in aliquots at –80°C. Repeated freeze and thaw cycles will cause loss of activity. Under recommended storage conditions, product is stable for at least one year.
References 1. Kock, M et al; Structure and Function of Recombinant Cobra Venom Factor. J Biol Chem 2004, 279: 30836

2. Vogel, C et al; Recombinant cobra venom factor. Molecular immunology 2004, 41:191

3. Vogel, C et al; Humanized cobra venom factor: Structure, activity, and therapeutic efficacy in preclinical disease models. Mol Immunol 2014, 61:191

Precautions For research use only. Not for use in or on humans or animals or for diagnostics. It is the responsibility of the user to comply with all local/state and federal rules in the use of this product. Hycult Biotech is not responsible for any patent infringements that might result from the use or derivation of this product.
Applications
Application: Functional studies, Western blot
Application notes: Dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions.

W: A reduced sample treatment and SDS-Page was used. The band size is ~150 kDa.

FS: Complement activation after incubation with CVF is tested by the lysis of sheep red blood cells.
References
References: 1. Kock, M et al; Structure and Function of Recombinant Cobra Venom Factor. J Biol Chem 2004, 279: 30836

2. Vogel, C et al; Recombinant cobra venom factor. Molecular immunology 2004, 41:191

3. Vogel, C et al; Humanized cobra venom factor: Structure, activity, and therapeutic efficacy in preclinical disease models. Mol Immunol 2014, 61:191

Product information English
CoA-TDS Protein
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