Analytical Data
-
Gene name
Rpl7
- Application
-
Alternative Names
Rpl7；Large ribosomal subunit Protein uL30
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P18124
-
Expression Region
1-248aa
-
AA Sequence
MEGVEEKKKE VPAVPETLKK KRRNFAELKI KRLRKKFAQK MLRKARRKLI YEKAKHYHKE YRQMYRTEIR MARMARKAGN FYVPAEPKLA FVIRIRGING VSPKVRKVLQ LLRLRQIFNG TFVKLNKASI NMLRIVEPYI AWGYPNLKSV NELIYKRGYG KINKKRIALT DNALIARSLG KYGIICMEDL IHEIYTVGKR FKEANNFLWP FKLSSPRGGM KKKTTHFVEG GDAGNREDQI NRLIRRMN
-
Molecular Weight
29.2 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
Rpl7, a pivotal component of the ribosomal large subunit, plays a crucial role in protein synthesis and ribosome assembly. It is a universally conserved protein found across various organisms, highlighting its fundamental importance in cellular biology. Research into Rpl7 has gained momentum due to its involvement in various cellular processes, including cell growth, proliferation, and stress response. Abnormalities in Rpl7 expression or functionality have been linked to several diseases, including cancer, where ribosomal biogenesis and protein synthesis are often dysregulated.
The study of recombinant Rpl7 proteins offers valuable insights into their structure-function relationships, enabling researchers to dissect the molecular mechanisms underlying ribosome assembly and function. Additionally, understanding how Rpl7 interacts with other ribosomal proteins and rRNA is essential for elucidating the dynamics of ribosome formation and its influence on cellular homeostasis. As ribosomes are the site of protein synthesis, the exploration of Rpl7 could also pave the way for novel therapeutic strategies aimed at rectifying ribosomal dysfunctions in diseases. Consequently, the research on Rpl7 recombinant proteins not only enhances our understanding of ribosomal biology but also has significant implications for medical science and therapeutic development.
