Analytical Data
-
Gene name
PGGT1b
- Application
-
Alternative Names
GGTI; BGGI; GGTase 1 β-subunit; Type I protein geranyl-geranyltransferase subunit beta
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P53609
-
Expression Region
Met1~Thr377
-
Molecular Weight
44kDa
-
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
PGGT1b, or protein geranylgeranyltransferase type I beta, is an enzyme that plays a crucial role in the post-translational modification of proteins through the addition of geranylgeranyl groups. This modification is vital for the proper membrane localization and function of various signaling proteins, including many small GTPases that are involved in cell growth, differentiation, and survival. The dysregulation of PGGT1b and the pathways it influences has been implicated in several diseases, particularly cancer, where aberrant protein localization can lead to uncontrolled cell proliferation and tumor progression. Research on PGGT1b recombinant protein has gained significant attention due to its potential as a therapeutic target in malignancies driven by altered signaling pathways. By studying the structure-function relationship of PGGT1b, scientists aim to develop inhibitors that can specifically disrupt its activity, thereby providing a novel approach to more effective cancer treatments. Furthermore, understanding the enzymatic mechanism and substrate specificity of PGGT1b offers insights into the broader family of prenyltransferases and their roles in other diseases, including cardiovascular disorders and neurodegenerative conditions. Overall, the continued investigation of PGGT1b and its recombinant forms is essential for unraveling its complex biological functions and advancing potential clinical applications.
