Analytical Data
-
Gene name
KLK9
- Application
-
Alternative Names
KLK9；Kallikrein-9
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UKQ9
-
Expression Region
16-250aa
-
AA Sequence
HGWADTRAIGAEECRPNSQPWQAGLFHLTRLFCGATLISDRWLLTAAHCRKPYLWVRLGEHHLWKWEGPEQLFRVTDFFPHPGFNKDLSANDHNDDIMLIRLPRQARLSPAVQPLNLSQTCVSPGMQCLISGWGAVSSPKALFPVTLQCANISILENKLCHWAYPGHISDSMLCAGLWEGGRGSCQGDSGGPLVCNGTLAGVVSGGAEPCSRPRRPAVYTSVCHYLDWIQEIMEN
-
Molecular Weight
32.0 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
KLK9, or Kallikrein-related peptidase 9, is a member of the kallikrein family of serine proteases that plays a significant role in various physiological and pathological processes, including tissue remodeling, inflammation, and cancer progression. Studies have shown that KLK9 is differentially expressed in various cancer types, particularly in prostate cancer, where it has been implicated in tumor growth and metastasis. The ability of KLK9 to cleave specific substrates suggests it may be involved in the activation of growth factors or other proteases, highlighting its potential role in the tumor microenvironment. Furthermore, KLK9's expression levels and enzymatic activity may serve as biomarkers for cancer diagnosis and prognosis. Given its importance in cancer biology, researchers have turned towards the production of recombinant KLK9 proteins to elucidate its biological functions and mechanisms of action. The recombinant protein can be utilized in in vitro studies to investigate its enzymatic activity, substrate specificity, and potential interactions with various signaling pathways. Moreover, generating KLK9 as a recombinant protein provides opportunities to explore its therapeutic applications, particularly in developing targeted therapies that aim to inhibit its activity in tumor progression. Understanding the functional roles of KLK9 through recombinant research may contribute to the development of novel diagnostic tools and treatment strategies in oncology, making it an important focus of contemporary biomedical research.
