Analytical Data
-
Gene name
rplL
- Application
-
Alternative Names
rplL；Large ribosomal subunit Protein bL12
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
B1IUR1
-
Expression Region
1-121aa
-
AA Sequence
MSITKDQIIEAVAAMSVMDVVELISAMEEKFGVSAAAAVAVAAGPVEAAEEKTEFDVILKAAGANKVAVIKAVRGATGLGLKEAKDLVESAPAALKEGVSKDDAEALKKALEEAGAEVEVK
-
Molecular Weight
19.2 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
The RplL protein, a component of the ribosomal large subunit, plays a crucial role in protein synthesis across various organisms. Research on RplL has gained prominence due to its involvement in regulating translation and maintaining ribosomal integrity, which are vital for cell growth and metabolism. Studies have demonstrated that mutations or dysfunctions in ribosomal proteins, including RplL, are often linked to various diseases, such as cancer and genetic disorders, by affecting protein synthesis and cellular functions. Consequently, understanding the structure, function, and regulation of RplL can provide insights into the molecular mechanisms underpinning these diseases. Additionally, RplL has been a focus of interest in the field of antibiotic research, as it serves as a potential target for developing new antimicrobial agents. Elucidating the interactions between RplL and other ribosomal components or inhibitors can pave the way for novel therapeutic approaches. Thus, investigating RplL not only enhances our understanding of fundamental biological processes but also holds significant implications for medical science and drug development.
