Q: I am trying to establish a method to measure mice C3 levels by nephelometry. I would be most grateful if you could provide me with some help, regarding the choice of the Ab. I totally understand that since such a method has never been tried, I do not expect any guaranties.

A: We have never performed nephelometry in our lab, and do not have a protocol or advice to provide about this application. However, it seems to me that you should choose an antibody that is capable of recognizing its target in its folded conformation. Therefore, I would suggest trying an antibody that has been validated for ICC or IHC.

Recombinant Human Complement C3 GST (N-Term) Protein

Novus Biologicals | Catalog # H00000718-Q01

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Product Specifications
Scientific Data
Preparation & Storage
Background
Product Documents
Specific Notices
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Key Product Details

Source

Wheat germ

Tag

GST (N-Term)

Applications

Western Blot, ELISA, Affinity Purification, Microarray

View all Complement C3 Proteins and Enzymes »

Product Specifications

Description

A recombinant protein with a N-terminal GST tagcorresponding to the amino acids 1-111 of Human C3

Source: Wheat Germ (in vitro)

Amino Acid Sequence: DKACEPGVDYVYKTRLVKVQLSNDFDEYIMAIEQTIKSGSDEVQVGQQRTFISPIKCREALKLEEKKHYLMWGLSSDFWGEKPNLSYIIGKDTWVEHWPEEDECQDEENQK

Purity

>80% by SDS-PAGE and Coomassie blue staining

Activity

This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated.

Protein / Peptide Type

Recombinant Protein

Scientific Data Images for Recombinant Human Complement C3 GST (N-Term) Protein

SDS-PAGE: Recombinant Human Complement C3 GST (N-Term) Protein [H00000718-Q01]

SDS-Page: Complement C3 Partial Recombinant Protein [H00000718-Q01]

Formulation, Preparation, and Storage

H00000718-Q01

Preparation Method	in vitro wheat germ expression system
Formulation	50 mM Tris-HCI, 10 mM reduced Glutathione, pH 8.0 in the elution buffer.
Preservative	No Preservative
Concentration	Please see the vial label for concentration. If unlisted please contact technical services.
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage	Store at -80C. Avoid freeze-thaw cycles.

Background: Complement C3

The complement system, or complement cascade, is a part of the innate immune system that assists in defense against pathogens (1-3). Complement C3, also called C3 or C3 protein, is one of nine complement proteins and is the main component of the complement system which is composed of over 30 soluble and membrane-bound proteins (1,4). The complement cascade consists of three main pathways: the classical, the lectin, and the alternative, all of which converge into a common pathway involving C3 cleavage by C3-convertases (1-6). Human Complement C3 is synthesized as a protein of 1663 amino acids (aa) in length with a theoretical molecular weight of ~185 kDa (5). Complement C3 is the most prevalent human complement protein in the serum, with a concentration of 1.2 mg/mL, and is predominantly produced by hepatocytes in the liver, but is also synthesized by blood cells and epithelial cells (3,5). Furthermore, the structure of C3 is comprised of an alpha-chain (110 kDa) and a beta-chain (75 kDa) linked by a disulfide bond (5). Cleavage of inactive C3 by C3-convertases produces active C3a, which functions as a mediator of inflammation, and C3b, which is an opsonin (1-4). In addition to amplification of complement response, C3 fragments serve multiple additional functions including chemotaxis, phagocytosis, adhesion, and immune modulation (3). Complement C3 serves dual purposes where it is involved in pathogenesis and immunity but, conversely, cellular damage results from unregulated C3 activation (5).

Both elevated levels and reduced levels of Complement C3 has been implicated in diseases pathologies (6). Deficiency in Complement proteins can result in autoimmune disorders including systemic lupus erythematosus, which is more often associated with C1 or C4 deficiency and only rarely with C3 deficiency (6). However, C3 deficiency typically results in increased risk of recurrent bacterial infections and glomerulonephritis, characterized by inflammation of the filtering glomeruli in the kidneys (6). Additionally, elevated levels of C3a and C4a is seen in patients with antiphospholipid antibody syndrome (6). Serum levels of C3 are also higher in rheumatoid arthritis cases (6). The complement system has become a target for drugs and therapeutics aimed at modulating innate immunity (7). For instance, compstatin is a peptide that binds to C3, inhibiting convertase activity and cleavage and can be used to treat diseases associated with uncontrolled C3 activation (7). C3-inhibitors and other complement inhibitors are a promising drug candidate for treatment of many diseases (7).

References

1. Mathern, D. R., & Heeger, P. S. (2015). Molecules Great and Small: The Complement System. Clinical Journal of the American Society of Nephrology: CJASN. https://doi.org/10.2215/CJN.06230614

2. Merle, N. S., Church, S. E., Fremeaux-Bacchi, V., & Roumenina, L. T. (2015). Complement System Part I - Molecular Mechanisms of Activation and Regulation. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2015.00262

3. Ricklin, D., Reis, E. S., Mastellos, D. C., Gros, P., & Lambris, J. D. (2016). Complement component C3 - The "Swiss Army Knife" of innate immunity and host defense. Immunological Reviews. https://doi.org/10.1111/imr.12500

4. Merle, N. S., Noe, R., Halbwachs-Mecarelli, L., Fremeaux-Bacchi, V., & Roumenina, L. T. (2015). Complement System Part II: Role in Immunity. Frontiers in Immunology. https://doi.org/10.3389/fimmu.2015.00257

5. Sahu, A., & Lambris, J. D. (2001). Structure and biology of complement protein C3, a connecting link between innate and acquired immunity. Immunological Reviews. https://doi.org/10.1034/j.1600-065x.2001.1800103.x

6. Vignesh, P., Rawat, A., Sharma, M., & Singh, S. (2017). Complement in autoimmune diseases. Clinica Chimica Acta; International Journal of Clinical Chemistry. https://doi.org/10.1016/j.cca.2016.12.017

7. Mastellos, D. C., Yancopoulou, D., Kokkinos, P., Huber-Lang, M., Hajishengallis, G., Biglarnia, A. R., Lupu, F., Nilsson, B., Risitano, A. M., Ricklin, D., & Lambris, J. D. (2015). Compstatin: a C3-targeted complement inhibitor reaching its prime for bedside intervention. European Journal of Clinical Investigation. https://doi.org/10.1111/eci.12419

Alternate Names

Acylation Stimulating Protein, acylation-stimulating protein cleavage product, AHUS5, ARMD9, ASP, C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3a, C3a anaphylatoxin, C3adesArg, C3b, C3bc, C3-beta-c, complement C3, Complement C3 alpha chain, Complement C3 beta chain, Complement C3b alpha' chain, Complement C3c alpha' chain fragment 1, Complement C3c alpha' chain fragment 2, Complement C3d fragment, Complement C3dg fragment, Complement C3f fragment, Complement C3g fragment, complement component 3, complement component C3, complement component C3a, complement component C3b, CPAMD1, EC 3.4.21.43, epididymis secretory sperm binding protein Li 62p, HEL-S-62p, prepro-C3

Gene Symbol

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Product Specific Notices for Recombinant Human Complement C3 GST (N-Term) Protein

This product is produced by and distributed for Abnova, a company based in Taiwan.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

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