Analytical Data
-
Gene name
C1D
- Application
-
Alternative Names
C1D；Nuclear nucleic acid-binding Protein C1D
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q13901
-
Expression Region
1-141aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAGEEIN EDYPVEIHEY LSAFENSIGA VDEMLKTMMS VSRNELLQKL DPLEQAKVDL VSAYTLNSMF WVYLATQGVN PKEHPVKQEL ERIRVYMNRV KEITDKKKAG KLDRGAASRF VKNALWEPKS KNASKVANKG KSKS
-
Molecular Weight
18 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
C1D, a member of the RIO kinase family, has garnered significant interest in recent years due to its potential role in various cellular processes, including cell proliferation, apoptosis, and DNA damage response. Research indicates that C1D may be involved in the regulation of chromatin structure and function, influencing gene expression and transcriptional regulation. Its overexpression has been linked to several cancers, suggesting that it may act as an oncogene, thereby offering potential as a therapeutic target. The study of C1D recombinant protein has become critical for understanding its molecular mechanisms and interactions within the cell. The use of recombinant techniques allows for the production of this protein in a controlled environment, enabling detailed biochemical and biophysical characterization. This research, therefore, not only aims to illuminate the fundamental biological roles of C1D but also seeks to explore its implications in cancer biology, potentially paving the way for novel therapeutic strategies. Additionally, understanding the structure-function relationship of C1D can provide insights into its regulatory mechanisms and interactions with other cellular proteins, further establishing its significance in the context of cellular health and disease.
