C3 antibody
GTX14232
ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry
Product group Antibodies
TargetC3
Overview
- SupplierGeneTex
- Product NameC3 antibody
- Delivery Days Customer9
- ApplicationsImmunoFluorescence, Western Blot, ELISA, ImmunoCytoChemistry, ImmunoHistoChemistry
- CertificationResearch Use Only
- ClonalityPolyclonal
- ConjugateUnconjugated
- Gene ID718
- Target nameC3
- Target descriptioncomplement C3
- Target synonymsacylation-stimulating protein cleavage product; AHUS5; ARMD9; ASP; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; C3a; C3a anaphylatoxin; C3b; complement C3; complement component 3; complement component C3a; complement component C3b; CPAMD1; epididymis secretory sperm binding protein Li 62p; HEL-S-62p; prepro-C3
- HostChicken
- IsotypeIgY
- Protein IDP01024
- Protein NameComplement C3
- Scientific DescriptionThe complement factor C3 consists of an alpha and a beta chain. C3 is a central factor in the complement cascade. It is central to the alternative pathway that leads to the C3 convertase C3bBb. The classical mannose binding lectin activation pathway leads to the C3 convertase C4b2a. These convertases cleave C3 resulting in C3a andC3b. Further degradation leads to the formation of the alpha chain products C3d, C3g and C3c. C3 is an acute phase protein that is produced by a wide range of tissues, including renal epithelial cells and hepatocytes.
- Storage Instruction-20°C or -80°C,2°C to 8°C
- UNSPSC12352203

![The two groups of complement C3 proteins can be purified by GTX02807 C3 antibody [M68] immunoaffinity chromatography from the partially purified milk fractions. Human milk proteins were loaded onto CM-Sepharose 4B column and proteins, including C3, were eluted by different salt (NaCl) concentration. The slat concentration was smaller than 0.3 N. The CM low salt fractions were collected and loaded to the mAb M68-Sepharose column to purify C3. After washing the immunoaffinity column, the captured proteins were eluted by 0.1 N glycine buffer pH 2.4. The eluates were collected into several fractions, E1, E2, E3, E4, E5 and E6. E1-E4 fractions were analyzed by SDS-PAGE and the eluted proteins were stained by CBB. The protein band 2 and 7 as indicated are sliced out and subjected to MS/MS protein identification (by Prottech Inc.), confirming these bands to be complement C3. The relative abundance of peptides matching to C3 is 98% for band 2 and 96% for band 7. For the best detection sensitivity, the samples should be treated under non-boiled and non-reducing conditions. Lane A : Input (partially purified milk fractions) Lane B : Flow through Lane C : Elution 1 Lane D : Elution 2 Lane E : Elution 3 Lane F : Elution 4 Loading : 20 microl](https://www.genetex.com/upload/website/prouct_img/normal/GTX02807/GTX02807_20201130_IP_w_23053122_193.webp)

