C3 is the most abundant complement protein in guinea pig serum.
Its biological function strongly resembles that of C3 in man and other laboratory animal species.
It has a central role in the activation system being common in both pathways.
Activation of C3 is achieved by specific limited proteolysis resulting in the increase of a number of degradation fragments.
The anaphylatoxin C3a promotes smooth muscle contraction and increases vascular permeability; the large C3b fragment is involved in binding to the complement activator and can interact with specific receptors to allow efficient clearance of the activating cell or particle; degradation fragments of C3b (C3bi, C3c, C3dg and C3d) are important in receptor binding and clearance mechanisms, in virus neutralization and possible in the immune response.
Applications:Suitable for use in IEP, Single and Double RID.
Other applications have not been tested.
Recommended Dilutions: IEP: Use 2ul serum, plasma or equivalent against 120ul antiserum
Double RID: Use a rosette arrangement with 10ul antiserum in a 3mm diameter center well and 2ul serum samples (neat and serially diluted) in 2mm diameter peripheral wells
SIngle RID: use 1% antiserum in the gel
Optimal dilutions to be determined by the researcher.
Storage and Stability:Lyophilized powder may be stored at -20°C.
Stable for 12 months at -20°C.
Reconstitute with sterile ddH2O.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Reconstituted product is stable for 12 months at -20°C.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Further dilutions can be made in assay buffer.
仕様
Size：1ml
Host：rabbit
Source Antibody：guinea pig
Grade：Serum
Purity：Serum
Form：Supplied as a lyophilized powder. No preservatives added. Reconstitute with 1ml sterile ddH2O. Dilute further with PBS, pH 7.2.
Specificity：Recognizes guinea pig Complement C3, C3c subunit. In IEP against fresh guinea pig serum, a single precipitin line is obtained in the beta-1 region representing native C3. Against serum containing partly activated C3, a precipitin line is obtained which extends from the beta-1 into the alpha-2 region, demonstrating a gradient. In old serum containing totally activated C3 a single precipitin line in the alpha-2 region is obtained.
