Analytical Data
-
Gene name
clfA
- Application
-
Alternative Names
clfA;IF;Complement factor I
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5HHM8
-
Expression Region
229-559aa
-
AA Sequence
GTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKDDVKATLTMPAYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNIIWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPE
-
Molecular Weight
37.5 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The clfA gene, encoding the fibrinogen-binding protein ClfA, is an important virulence factor in Staphylococcus aureus, a pathogenic bacterium responsible for a wide range of human infections. ClfA plays a crucial role in the adherence of S. aureus to host tissues by binding to fibrinogen, thereby facilitating the formation of biofilms and contributing to the bacterium's ability to evade the immune response. Given the increasing incidence of antibiotic-resistant strains of S. aureus, including methicillin-resistant Staphylococcus aureus (MRSA), there is a pressing need for novel therapeutic strategies. The recombinant expression of ClfA offers a valuable approach to studying its structure-function relationship, immune response elicitation, and potential as a target for vaccine development. By producing ClfA as a recombinant protein, researchers can assess its functionality in vitro, elucidate its role in pathogenicity, and explore its potential as a biomarker for infection. Furthermore, understanding the immunogenic properties of ClfA could pave the way for the development of innovative immunotherapies to enhance host defense mechanisms against S. aureus infections. This research is not only crucial for the advancement of microbiology and immunology but also has significant implications for public health, especially in the context of rising antibiotic resistance and the increasing burden of staphylococcal diseases.











