Baby rabbit complement serum preparation is intended for use as a source of rabbit complement for cytotoxicity studies.
- Product Form
Pack Size: 1 ml
Baby rabbit serum - lyophilized
Pack Size: 2 ml
Baby rabbit serum - lyophilised
Pack Size: 1 ml
Reconstitute with 1.0 ml ice cold distilled water
Pack Size: 2 ml
Reconstitute with 2ml ice cold distilled water
- Preservative Stabilisers
- None present
- Prior to reconstitution store at +4oC. Following reconstitution store at +4oC for 1 hour or aliquot and store at -70oC for longer.
This product should be stored undiluted. Avoid repeated freezing and thawing as this may denature the product. Should this product contain a precipitate we recommend microcentrifugation before use.
- Guaranteed until date of expiry. Please see product label.
- For research purposes only
This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Applications of Baby Rabbit Complement
|Functional Assays 1
- 1 This product is not sold as sterile but can be sterilized by filtration if necessary. It is preferable to dilute the complement to a final working concentration before filtration in order to minimize loss of volume.
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
- Instructions For Use
- Use within one hour of reconstitution, keeping on ice throughout.
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Application Based External Images
Product Specific References
References for Baby Rabbit Complement
Council of Europe. (1983) Essential aspects of tissue typing: Preparation, use, storage of reagents and standardisation of complement.
European Health Committee, Strasbourg, ISBN 92-871.224-4.
Edited by J.G.Ray. (1979) NIAID Manual of tissue typing techniques.
Publication No. NIH-80-545.
Anderson, L.D. Jr et al. (1999) Enhancement of graft-versus-tumor activity and graft-versus-host disease by pretransplant immunization of allogeneic bone marrow donors with a recipient-derived tumor cell vaccine.
Cancer Res. 59 (7): 1525-30.
Mason, J.C. et al. (2002) Statin-induced expression of decay-accelerating factor protects vascular endothelium against complement-mediated injury.
Circ Res. 91 (8): 696-703.
Lidington, E.A. et al. (2000) Induction of decay-accelerating factor by thrombin through a protease-activated receptor 1 and protein kinase C-dependent pathway protects vascular endothelial cells from complement-mediated injury.
Blood. 96 (8): 2784-92.
De clercq, L. et al. (1997) An anti-adipocyte monoclonal antibody is cytotoxic to porcine preadipocytes in vitro and depresses the development of pig adipose tissue.
J Anim Sci. 75 (7): 1791-7.
Hung, M.C. et al. (2011) The Neisseria meningitidis Macrophage Infectivity Potentiator Protein Induces Cross-Strain Serum Bactericidal Activity and Is a Potential Serogroup B Vaccine Candidate.
Infect Immun. 79: 3784-91.
Lee, S.J. et al. (2012) Identification of a common immune signature in murine and human systemic Salmonellosis.
Proc Natl Acad Sci U S A. 109 (13): 4998-5003.
Goh, Y.S. & MacLennan, C.A. (2013) Invasive African nontyphoidal Salmonella requires high levels of complement for cell-free antibody-dependent killing.
J Immunol Methods. 387 (1-2): 121-9.
Li, S.H. et al. (2004) C-reactive protein upregulates complement-inhibitory factors in endothelial cells.
Circulation. 109: 833-6.
Hyams, C. et al. (2010) Streptococcus pneumoniae resistance to complement-mediated immunity is dependent on the capsular serotype.
Infect Immun. 78: 716-25.
Newcombe, J. et al. (2004) Infection with an avirulent phoP mutant of Neisseria meningitidis confers broad cross-reactive immunity.
Infect Immun. 72: 338-44.
Mason, J.C. et al. (2002) bFGF and VEGF synergistically enhance endothelial cytoprotection via decay-accelerating factor induction.
Am J Physiol Cell Physiol. 282: C578-87.
Sancho, D. et al. (2006) CD69 targeting differentially affects the course of collagen-induced arthritis.
J Leukoc Biol. 80: 1233-41.
Hung MC et al. (2013) The adhesin complex protein (ACP) of Neisseria meningitidis is a new adhesin with vaccine potential.
MBio. 4 (2): pii: e00041-13.
Goh YS et al. (2016) Bactericidal Immunity to Salmonella in Africans and Mechanisms Causing Its Failure in HIV Infection.
PLoS Negl Trop Dis. 10 (4): e0004604.
Sawant S et al. (2016) Establishment of 3D Co-Culture Models from Different Stages of Human Tongue Tumorigenesis: Utility in Understanding Neoplastic Progression.
PLoS One. 11 (8): e0160615.
Humbert MV et al. (2016) Vaccine Potential and Diversity of the Putative Cell Binding Factor (CBF, NMB0345/NEIS1825) Protein of Neisseria meningitidis.
PLoS One. 11 (8): e0160403.
Nganje, C.N. et al. (2019) PepN is a non-essential, cell wall-localized protein that contributes to neutrophil elastase-mediated killing of Streptococcus pneumoniae.
PLoS One. 14 (2): e0211632.
Dierckx de Casterlé I et al. (2018) Reduction of myeloid-derived suppressor cells reinforces the anti-solid tumor effect of recipient leukocyte infusion in murine neuroblastoma-bearing allogeneic bone marrow chimeras.
Cancer Immunol Immunother. 67 (4): 589-603.
Cuesta-Mateos, C. et al. (2020) CCR7 as a novel therapeutic target in t-cell PROLYMPHOCYTIC leukemia
Biomarker Research.8, 54.
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