Analytical Data
-
Gene name
CPB2
- Application
-
Alternative Names
CPB2；Cytochrome P450 2B6
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96IY4
-
Expression Region
1-423aa
-
AA Sequence
MKLCSLAVLV PIVLFCEQHV FAFQSGQVLA ALPRTSRQVQ VLQNLTTTYE IVLWQPVTAD LIVKKKQVH FFVNASDVDN VKAHLNVSGI PCSVLLADVE DLIQQQISND TVSPRASASY YEQYHSLNE IYSWIEFITE RHPDMLTKIH IGSSFEKYPL YVLKVSGKEQ AAKNAIWIDC GIHAREWIS PAFCLWFIGH ITQFYGIIGQ YTNLLRLVDF YVMPVVNVDG YDYSWKKNRM WRKNRSFYA NNHCIGTDLN RNFASKHWCE EGASSSSCSE TYCGLYPESE PEVKAVASFL RRNINQIKA YISMHSYSQH IVFPYSYTRS KSKDHEELSL VASEAVRAIE KTSKNTRYTH GHGSETLYL APGGGDDWIY DLGIKYSFTI ELRDTGTYGF LLPERYIKPT CREAFAAVSK IAWHVIRNV
-
Molecular Weight
47 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
CPB2, a key member of the cysteine protease family, is primarily derived from the parasitic organism *Cryptosporidium parvum*, which poses significant challenges to global health as a leading cause of waterborne gastrointestinal infections. The role of CPB2 in the pathogenicity of *C. parvum* has attracted substantial attention, particularly given its implication in the modulation of host immune responses. Research into CPB2 involves the exploration of its structure and function, aiming to understand how this enzyme contributes to the parasite's lifecycle and virulence. Additionally, CPB2 is recognized for its potential as a therapeutic target or vaccine candidate, due to its essential role in parasite survival and the immune evasion mechanisms it employs. Advances in recombinant protein technology have enabled the production of active CPB2 for detailed biochemical and immunological studies, facilitating investigations into its substrate specificity and potential inhibitory compounds. The findings from these studies could not only provide insights into *C. parvum* pathogenesis but also pave the way for novel intervention strategies against cryptosporidiosis, especially in immunocompromised populations. As research progresses, understanding the precise mechanisms of CPB2 activity may aid in the development of more effective treatments and prevention methods to combat this pervasive infectious disease.
