Absolute Antibody is developing engineered antibodies for the research and diagnostics markets. Unlike hybridoma-manufactured antibodies, recombinant antibodies can be reformatted to different species, isotypes, and subtypes. This approach allows us to better control antibody performance in vivo.
We have compiled a list of antibodies against cell surface molecules with potential applications in in vivo research below. The VivopureTM range is available at a range of bulk quantities and competitively priced.
- available at 10 mg, 25 mg and 100 mg in addition to standard measures
- guaranteed low endotoxin levels < 1.0 EU/mg (LAL method)
- > 98% reagent purity with no serum contaminants (SDS-PAGE)
- delivered in PBS with no added preservatives
The importance of the Fc Domain in vivo
The IgG Fc domain (constant) of an antibody determines its binding properties to Fc gamma receptors (FcγR, FcR) and complement factors (C1q). Changing antibody subtype may therefore mediate downstream effector function, summarised in part in Table 1 for human and mouse IgG subtyoes. For example, human IgG1 displays high antibody dependent cell-mediated cytotoxicity (ADCC) and complement-dependant cytotoxicity (CDC), and is the most suitable subtype for cytotoxic therapeutic use. Where cytotoxicity is not desirable, IgG2 and IgG4 antibodies would be preferable.
|Effector Function||Species||IgG Subtype Potency|
IgG Subtypes: There are four IgG subtypes in human (IgG1, IgG2, IgG3, IgG4), mouse (IgG1, IgG2a, IgG2b, IgG3) and rat (IgG1, IgG2a, IgG2b, IgG2c). IgG subtypes exhibit high sequence homology but unique FcγR and the C1q binding profiles.
Information compiled from : Schumaker et al. (1976) PMID: 990273; Burton (1984) PMID: 3889592; Unkeless et al. (1988) PMID: 2968084; Bruggemann et al. (1989) PMID: 3500259; Bindon et al. (1988) PMID: 3260935; Niwa et al. (2005) PMID: 16219319; Natsume et al. (2008) PMID: 18483271
Customization services offered by Absolute Antibody
- IgG subtype switching
Replacing Fc domain of antibody whilst maintaining the variable, antigen binding regions to tailor antibody to your specific research needs.
- Nullifying Effector Function
Abolish binding of Fc domain to FcγR using our Fc Silent™ Fc variant, a genetically engineered Fc domain developed at Absolute Antibody (patent in progress).
- Extending the Plasma Half-life
Mutations at the interface between the CH2 and CH3 domains can enhance IgG1 serum half-life in vivo. At Absolute Antibody we can facilitate your research tailoring the plasma half-life of any of our catalogue antibodies or an antibody based on sequences provided by customers.
- Species Switching
Our chimeric antibodies (cAbs) made by fusing the antigen binding regions from one species like mouse, with the constant domain (effector region) from another species such as a rat to increase compatibility of reagents between species and reduce unwanted immune reactions.
- Fc-fusion Proteins
Customers may also be interested in our range of Fc fusion proteins for in vivo research.
For orders over 100 mg, custom requests or for any other inquiry please contact us and we will be happy to help you.
|Product Name||Expected Species Reactivity||Applications|
|Anti-CD3 epsilon [145-2C11]|
|FC; WB; IP; activation|
|Anti-CD4 epitope A [YTS 191.1]|
|Anti-CD4 epitope B [YTA 3.1]|
|FC; IF; IHC|
|Anti-CD5 [YTS 121.5.2]|
|Anti-CD52 [YTH 34.5-G2b (Campath-1G)]|
Human; Rhesus Monkey
|Cytotoxicity Assay; ELISA; IHC-Fr; IHC-P; in vivo; FC; WB|
|Block; IP; FC; IHC|
|Anti-Complement Receptor 1 & 2 [7G6]|
|FC; IHC-Fr; IP; WB; Block; CoStim|
|IHC; in vivo; FC; IF|
|ELISA; FC; in vivo; IHC|
|FC; IP; WP; IHC; Block|
|Anti-Nerve Growth Factor [αD11]|
|IF; Block; ELISA; IHC|
|Anti-Thy-1 [YTS 188.8.131.52]|