Analytical Data
-
Gene name
CIR
- Application
-
Alternative Names
KCNJ5; GIRK4; G protein-activated inward rectifier potassium channel 4; GIRK-4; Cardiac inward rectifier; CIR
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P48544
-
Expression Region
1-450aa
-
AA Sequence
MGKSFANFMCKKDFHPASKSNIKKVWMAEQKISYDKKKQEELMQQYLKEQESYDNRLLMGDERVKNGLNFMYEAPPGAKKENKEKEETEGETEYKFEWQKGAPREKYAKDDMNIRDQPFGIQVRNVRCIKCHKWGHVNTDRECPLFGLSGINASSVPTDGSGPSMHPSELIAEMRNSGFALKRNVLGRNLTANDPSQEYVASEGEEDPEVEFLKSLTTKQKQKLLRKLDRLEKKKKKKDRKKKKFQKSRSKHKKHKSSSSSSSSSSSSSSTETSESSSESESNNKEKKIQRKKRKKNKCSGHNNSDSEEKDKSKKRKLHEELSSSHHNREKAKEKPRFLKHESSREDSKWSHSDSDKKSRTHKHSPEKRGSERKEGSSRSHGREERSRRSRSRSPGSYKQRETRKRAQRNPGEEQSRRNDSRSHGTDLYRGEKMYREHPGGTHTKVTQRE
-
Molecular Weight
78.7 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
CIR (Cytoplasmic Inhibitor of Recombination) protein has garnered significant interest in the field of molecular biology due to its pivotal role in DNA repair and recombination processes. Its primary function is to regulate the activity of proteins involved in homologous recombination, a critical mechanism for maintaining genomic stability and facilitating proper DNA repair, particularly during cellular stress conditions such as DNA damage. Research indicates that the dysfunction or dysregulation of CIR can lead to increased susceptibility to genomic instability and has been implicated in various diseases, including cancer. Understanding the structure and function of CIR not only sheds light on fundamental cellular processes but also opens potential avenues for therapeutic interventions. By elucidating the molecular mechanisms through which CIR exerts its effects, scientists aim to develop novel strategies for enhancing DNA repair pathways in cancer therapy and improving the efficacy of existing treatments. This research potentially contributes to the development of biomolecular techniques that can manipulate CIR activity for improved patient outcomes, highlighting its significance in both basic research and clinical applications.











