anti-C1s� antibody product blog
Tags: Antibody; Monoclonal Antibody; C1s�; anti-C1s� antibody;
The C1s� c1s (Catalog #MBS2543886) is an Antibody produced from Rabbit and is intended for research purposes only. The product is available for immediate purchase. The Rabbit anti Human�C1s� Monoclonal Antibody reacts with Human and may cross-react with other species as described in the data sheet. MyBioSource\'s C1s� can be used in a range of immunoassay formats including, but not limited to, ELISA (EIA).ELISA: 0.1-0.2 mug/mL. This antibody can be used at 0.1-0.2 mug/mL with the appropriate secondary reagents to detect Human C1S. The detection limit for Human C1S is approximately 0.00245 ng/well. Researchers should empirically determine the suitability of the C1s� c1s for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The C1s� c1s product has the following accession number(s) (GI #41393602). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Complement is an integral component of the adaptive and innate immune systems and represents one of the major effector systems for the immune responses. The classical complement pathway is triggered by C1, a complex composed of the binding protein C1q and two proenzymes, C1r and C1s. Upon binding of IgG to the head of C1q, C1r undergoes autoactivation and in turn cleaves and activates C1s. C1r and C1s, the proteases responsible for activation and proteolytic activity of the C1 complex of complement, share similar overall structural organizations featuring five nonenzymic protein modules (two CUB modules surrounding a single EGF module, and a pair of CCP modules) followed by a serine protease domain. Besides highly specific proteolytic activities, both proteases exhibit interaction properties associated with their N-terminal regions. In contrast, C1r and C1s widely differ from each other by their glycosylation patterns: both proteins contain Asn-linked carbohydrates, but four glycosylation sites are present on C1r, and only two on C1s. As a highly specific serine protease, C1s executes the catalytic function of the C1 complex: the cleavage of C4 and C2, and thus instigates a sequence of activation steps of other components of the complement system, culminating in the formation of the membrane attack complex which induces cell lysis. Like other complement serine proteases C1s has restricted substrate specificity and it is engaged into specific interactions with other subcomponents of the complement system. The only other protein known to interact with C1s physiologically is SerpinC1, an inhibitor of serine protease, which inhibits C1s activity and thus plays a regulatory role in controlling the function of C1s enzyme.