Analytical Data
-
Gene name
VK1
- Application
-
Alternative Names
VK1;rpl25;rptL5;Large ribosomal subunit Protein bL25
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P45281
-
Expression Region
1-95aa
-
AA Sequence
MAFKFNAEVR TAQGKGASRR LRHNGQIPAI VYGGSEEPVS IILNHDELNN AQAHESFYSE VITLVVEGKE VAVKVQAMQR HPFKPKLVHI DFKRA
-
Molecular Weight
10.6 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
VK1 recombinant protein, derived from the Vitamin K-dependent proteins, has gained significant attention in biomedical research due to its potential therapeutic applications. Vitamin K plays a crucial role in various physiological processes, particularly in coagulation, bone metabolism, and cellular functions. The VK1 protein is known for its involvement in the synthesis of coagulation factors, which are essential for normal blood clotting. Recent studies have indicated that VK1 may also have non-coagulation related functions, including modulating inflammation and promoting cell survival, thereby implicating its potential in treating diseases such as osteoporosis and certain types of cancer. The recombinant production of VK1 allows for the generation of large quantities of the protein, which can be utilized for both basic research and in therapeutic interventions. By exploring its structure, function, and interactions at a molecular level, researchers aim to better understand the broader biological roles of VK1 and its derivatives, ultimately paving the way for innovative treatments that leverage its biological properties. The study of VK1 recombinant protein represents a promising frontier in the field of protein therapeutics, signaling the importance of further investigation into its mechanisms and efficacy in clinical applications.











