Analytical Data
-
Gene name
CAP3
- Application
-
Alternative Names
CAP3;CANP3;CANPL3;NCL1;Calpain-3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P50453
-
Expression Region
1-376aa
-
AA Sequence
METLSNASGTFAIRLLKILCQDNPSHNVFCSPVSISSALAMVLLGAKGNTATQMAQALSLNTEEDIHRAFQSLLTEVNKAGTQYLLRTANRLFGEKTCQFLSTFKESCLQFYHAELKELSFIRAAEESRKHINTWVSKKTEGKIEELLPGSSIDAETRLVLVNAIYFKGKWNEPFDETYTREMPFKINQEEQRPVQMMYQEATFKLAHVGEVRAQLLELPYARKELSLLVLLPDDGVELSTVEKSLTFEKLTAWTKPDCMKSTEVEVLLPKFKLQEDYDMESVLRHLGIVDAFQQGKADLSAMSAERDLCLSKFVHKSFVEVNEEGTEAAAASSCFVVAECCMESGPRFCADHPFLFFIRHNRANSILFCGRFSSP
-
Molecular Weight
69.4kDa
-
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
CAP3, or Cathelicidin Antimicrobial Peptide 3, is a key player in the innate immune response, particularly known for its role in host defense against various pathogens. The research surrounding CAP3 is driven by the increasing prevalence of antibiotic-resistant bacteria and the urgent need for novel antimicrobial agents. CAP3 is part of the cathelicidin family of peptides, which are produced by a wide range of organisms as a first line of defense. Studies have shown that CAP3 exhibits potent antibacterial, antiviral, and antifungal activities, making it a promising candidate for therapeutic applications. Its unique mechanism of action, which disrupts microbial membranes and inhibits microbial growth, sets it apart from traditional antibiotics. Moreover, CAP3 has been implicated in modulation of inflammation and wound healing, further enhancing its potential as a multifunctional therapeutic agent. Investigating the structure-function relationship of CAP3 and optimizing its stability and efficacy through recombinant protein technology has become a focal point for researchers. Understanding the biological pathways influenced by CAP3 can provide insights into developing new strategies for infection control and the treatment of inflammatory diseases. This research not only aims to uncover the mechanistic roles of CAP3 in immunity but also seeks to advance the field of peptide therapeutics, ultimately contributing to the fight against resistant pathogens and improving clinical outcomes for patients with infectious diseases.











