Analytical Data
-
Gene name
CTR
- Application
-
Alternative Names
CTR；ATRC2；CAT2；Cationic amino acid transporter 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P30988
-
Expression Region
1-474aa
-
AA Sequence
MRFTFTSRCLALFLLLNHPTPILPAFSNQTYPTIEPKPFLYVVGRKKMMDAQYKCYDRMQQLPAYQGEGPYCNRTWDGWLCWDDTPAGVLSYQFCPDYFPDFDPSEKVTKYCDEKGVWFKHPENNRTWSNYTMCNAFTPEKLKNAYVLYYLAIVGHSLSIFTLVISLGIFVFFRSLGCQRVTLHKNMFLTYILNSMIIIIHLVEVVPNGELVRRDPVSCKILHFFHQYMMACNYFWMLCEGIYLHTLIVVAVFTEKQRLRWYYLLGWGFPLVPTTIHAITRAVYFNDNCWLSVETHLLYIIHGPVMAALVVNFFFLLNIVRVLVTKMRETHEAESHMYLKAVKATMILVPLLGIQFVVFPWRPSNKMLGKIYDYVMHSLIHFQGFFVATIYCFCNNEVQTTVKRQWAQFKIQWNQRWGRRPSNRSARAAAAAAEAGDIPIYICHQELRNEPANNQGEESAEIIPLNIIEQESSA
-
Molecular Weight
55.3 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 study of CTR (Copper Transporter) recombinant proteins has emerged as a significant field of research due to the critical role of copper homeostasis in biological systems. Copper is an essential trace element required for various physiological functions, including enzymatic reactions involved in energy production, iron metabolism, and antioxidant defense. Dysregulation of copper levels can lead to a range of diseases, such as Wilson's disease and Menkes syndrome, which are characterized by defective copper transport and metabolism. Recombinant proteins, produced through genetic engineering techniques, allow for the detailed study of CTR function, structure, and interactions in a controlled environment. These proteins serve as vital tools for understanding the molecular mechanisms underlying copper transport and its implications in health and disease. Moreover, the ability to produce high quantities of pure CTR proteins facilitates the development of potential therapeutic strategies and diagnostic tools, making this area of research not only essential for basic science but also for clinical applications in treating copper-related disorders. The integration of biochemical, structural, and genetic approaches in CTR research continues to enhance our understanding of copper transport processes, paving the way for innovative insights into cellular metabolism and its impact on overall health.
