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Cobra Venum Factor Anticomplementary Protein

Certificate of Analysis and Data Sheet

Source:
Naja melanoleuca

Catalog No.
PRO-319

Background:

Cobra Venom Factor (CVF) is the complement-activating protein in cobra venom. Like C3b, CVF forms with factor B and factor D in human and mammalian serum the bimolecular C3/C5 convertase. This functional similarity of CVF and C3 correlates with many structural similarities, which led to the suggestion that CVF is evolutionally related to C3.

Description :

Cobra Venom Anticomplementary Protein has a molecular weight of 150kd and is used for immuno-suppression, decomplementing blood in vivo & in vitro, its dosage for mice is about 1ug per gram of body weight. CVF is purified by Affinity Column chromatography

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Solubility:

It is recommended to reconstitute the lyophilized Cobra Venum Factor in sterile 18MΩ-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Stability:

Lyophilized CVF although stable at room temperature for 3 weeks, should be stored desiccated below -18 C. Upon reconstitution CVF should be stored at 4 C between 2-7 days and for future use below -18 C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 90.0% as determined by:
(a)BCA protein assay.
(b)Polyacrylamide gel electrophoresis.
(c) SDS-PAGE Silver Stained gel showing the effect of pure CVF on the consumption of complement C3 in the blood of mice.

Dimers and aggregates:

Less than 1% as determined by silver-stained SDS-PAGE gel analysis.

Biological Activity:

Mice where given a single injection ( IP) of pure Cobra Venom Factor (purified from the venom of Naja melanoleuca or Naja kaouthia,25 ug/mice was injected) Blood sample was taken at the designated time intervals. SDS-PAGE immuno blot, using a C3 alpha chain specific antibody was used to demonstrate the consumption of C3 alpha chain in the blood. Both pure CVF from N. kaouthia and N. melanoleuca had the ability to activate the complement pathway, and to cause the depletion of complement in blood as is seen by the initial disappearance of the C3 alpha chain in the blood and the subsequent reappearance of newly synthesised C3 alpha chain.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.


Gene:

Name:C3

Protein synonyms/aliases:

Cobra venom factor precursor (CVF)
    (Complement C3 homolog)

Precursor's functional components:

Cobra venom factor alpha chain
Cobra venom factor gamma chain
Cobravenom factor beta chain .

Protein Family:


Protein Domains:


Domains:
IPR002890   Alpha-2-macroglobulin, N-terminal
IPR011625   Alpha-2-macroglobulin, N-terminal 2
IPR000020   Anaphylatoxin/fibulin
IPR001599   Alpha-2-macroglobulin
IPR011626   A-macroglobulin complement component
IPR011627   A-macroglobulin receptor
IPR001134   Netrin, C-terminal

Protein links:

Cobra Venum Factor Anticomplementary Protein protein domain

Cobra Venum Factor Anticomplementary Protein protein family


Precursor- Protein structure and amino acid sequence:


Latest Publications:

1. Preparation of complement fragments C3b and C3a from purified rat complement component C3 by activated cobra venom factor.
J Pharmacol Toxicol Methods 2005 Sep-Oct;52(2):260-3
2. Pre-treatment of donor with 1-deamino-8-d-arginine vasopressin could alleviate early failure of porcine xenograft in a cobra venom factor treated canine recipient.
Eur J Cardiothorac Surg 2005 Jul;28(1):149-56
3. The administration of cobra venom factor reduces post-ischemic cerebral injury in adult and neonatal rats.
Neurosci Lett 2005 May 20-27;380(1-2):48-53
4. [Mechanisms of purified cobra venom factor in preventing hyperacute rejection following discordant liver xenotransplantation in rats]
Zhonghua Yi Xue Za Zhi 2004 Dec 2;84(23):2007-10
5. Recombinant cobra venom factor.
Mol Immunol 2004 Jun;41(2-3):191-9
6. Functional analysis of Cobra Venom Factor/human C3 chimeras transiently expressed in mammalian cells.
Mol Immunol 2004 May;41(1):19-28

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中華民國95年06月06日更新