Analytical Data
-
Gene name
CH
- Application
-
Alternative Names
CH；Uncharacterized Protein C8orf48
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96LL4
-
Expression Region
1-319aa
-
AA Sequence
MAICPELAQTDKSALANLSDETETLKNSTDEVQTSSSFSSSGGRQSSPLTSGSKLEREKQTPSLEQGDTQSELLDYKNYEKKLSKKWINYLKLKDSNFERHQPDTKLPTEITRVSDEELNALQSYCTMKINLIHRRGDSKKKTSSRHKKLHLGLDVEASERDAFSCTVPDELLNRIYFKNMRTTPKQEAAAKQHISYQCPYCNRKRAELALSAFLKQKKTLLESFLLQERIDEHLHTKDFLTRIGEAHQDFPRLSDDPRIIWKRLTEKSHIRYSGFERSETEQKLQRDGNSACHLPFSLPFLKRLTLIKPELVIVNDNV
-
Molecular Weight
36.7 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 study of CH (chimeric heavy) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including therapeutics, diagnostics, and vaccine development. CH proteins are engineered to combine different functional domains from various proteins, enhancing their properties and functionalities. The ability to tailor these proteins allows researchers to optimize binding affinities, improve stability, and reduce immunogenicity. The advances in recombinant DNA technology and protein expression systems have facilitated the production of CH proteins in various host organisms, including bacteria, yeast, and mammalian cells. These advancements have not only streamlined the development process but also increased the yield and activity of the proteins produced. Furthermore, the versatility of CH proteins enables their use in targeted drug delivery systems, where they can be designed to specifically bind to certain cell types or tissues, thereby improving therapeutic efficacy and minimizing side effects. As research continues to delve into the intricate mechanisms of protein interactions and functionalities, CH recombinant proteins represent a promising frontier in biotechnology and medicine, offering innovative solutions to complex biological challenges.
