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AB229942

Anti-Cobra Venom Factor antibody

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(1 Publication)

Rabbit Polyclonal Cobra Venom Factor antibody. Suitable for WB and reacts with Recombinant full length protein - Monocled cobra samples. Cited in 1 publication. Immunogen corresponding to Recombinant Fragment Protein within Monocled cobra Cobra venom factor aa 700-1000.

View Alternative Names

Cobra venom factor, CVF, CVFk, Complement C3 homolog

1 Images
Western blot - Anti-Cobra Venom Factor antibody (AB229942)
  • WB

Supplier Data

Western blot - Anti-Cobra Venom Factor antibody (AB229942)

This protein is 185kDa before any post-translational modifications, but it can be split into 3 chains : alpha (aa 23-649), beta (aa 1264-1642) and gamma (aa 733-984). ab229942 detects the gamma chain.

All lanes:

Western blot - Anti-Cobra Venom Factor antibody (ab229942) at 1/500 dilution

Lane 1:

Cobra Venom Factor recombinant protein at 0.08 µg

Lane 2:

Cobra Venom Factor recombinant protein at 0.04 µg

Lane 3:

Cobra Venom Factor recombinant protein at 0.02 µg

Lane 4:

Cobra Venom Factor recombinant protein at 0.01 µg

Secondary

All lanes:

Goat polyclonal to rabbit IgG at 1/50000 dilution

Predicted band size: 185 kDa

Observed band size: 45 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Monocled cobra

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Monocled cobra Cobra venom factor aa 700-1000. The exact immunogen used to generate this antibody is proprietary information.

Q91132

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Monocled cobra": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Recombinant full length protein - Monocled cobra": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/500 - 1/5000", "WB-species-notes": "<p>This protein is 185kDa before any post-translational modifications, but it can be split into 3 chains: alpha (aa 23-649), beta (aa 1264-1642) and gamma (aa 733-984). The immunogen correspond to the gamma chain. Database link: <a data-tabindex-counter=\"1\" data-tabindex-value=\"none\" href=\"http://www.uniprot.org/uniprot/Q91132\" tabindex=\"-1\">Q91132</a></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purity >95%.
Storage buffer
pH: 7.4 Preservative: 0.03% Proclin 300 Constituents: PBS, 50% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cobra venom factor also known as gamma venom is a component found in the venom of certain cobra species. It has a molecular mass of approximately 150 kDa. This protein mimics the action of mammalian complement factor C3 and it expresses primarily in the venom glands of cobras. Cobra venom factor functions mechanically by binding to complement component C3 preventing its inactivation and leading to a depletion of complement components in the host organism. Scientists often investigate its role in immune modulation and envenomation.
Biological function summary

Complement pathways involve cobra venom factor through its interaction with the mammalian immune system. It acts by forming a stable complex with complement C3 and factor B leading to continuous activation without the normal regulatory inactivation processes. This results in consumption of complement proteins disrupting the complement system that is important (oops) for host defense. Such activities highlight its importance in immune evasion and modulation in the context of snakebite.

Pathways

Cobra venom factor intertwines with the complement cascade and immune response pathways. This factor significantly affects the classical and alternative complement pathways depleting complement components involved in opsonization and cell lysis. Proteins like complement C3 and factor B play important (oops) roles in these pathways interacting closely with cobra venom factor to sustain activation of the complement system providing insights into immune response manipulations.

Researchers study cobra venom factor's effects on conditions where complement consumption and dysregulation occur such as autoimmune diseases and inflammatory disorders. In systemic lupus erythematosus the depletion of complement components due to cobra venom factor's actions parallels observed clinical conditions where complement dysfunction contributes to pathogenesis. Additionally its association with complement proteins like C3 provides a model for understanding complement-related pathologies and potential therapeutic interventions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.
See full target information Cobra venom factor

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Cell death & disease 14:760 PubMed37993451

2023

The BRD4-SRPK2-SRSF2 signal modulates the splicing efficiency of ACSL3 pre-mRNA and influences erastin-induced ferroptosis in osteosarcoma cells.

Applications

Unspecified application

Species

Unspecified reactive species

Shun-Hong Luo,Jia-Ming Tian,Yi Chu,Hong-Yi Zhu,Jiang-Dong Ni,Jun Huang
View all publications

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