Analytical Data
-
Gene name
PHF11
- Application
-
Alternative Names
BRCA1 C-terminus-associated protein Renal carcinoma antigen NY-REN-34
-
Species
Human
-
Source
E. coli
-
Tag
N- GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UIL8
-
Expression Region
1-292aa
-
Molecular Weight
60.5 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
PHF11 (PHD finger protein 11) is a member of the PHD finger family, which is characterized by the presence of a specific zinc-binding motif. This protein has garnered attention due to its potential roles in various biological processes, including chromatin remodeling, gene regulation, and cell differentiation. Recent studies suggest that PHF11 may be implicated in immune responses and tumor biology, making it a target of interest for researchers exploring cancer and autoimmune diseases. Its unique structural features and functional implications in cellular signaling pathways highlight the need for understanding PHF11 at a molecular level. Recombination and expression of PHF11 can facilitate the study of its biochemical properties, interactions with other proteins, and its overall contribution to cellular homeostasis. Investigating PHF11 through recombinant protein studies could provide insights into its regulatory mechanisms and pave the way for therapeutic approaches targeting this protein in related diseases. As the field of protein research continues to advance, elucidating the roles of PHF11 within complex biological systems may offer novel perspectives on its function and therapeutic potential.
