Analytical Data
-
Gene name
NFYA
- Application
-
Alternative Names
NFYA;Nuclear transcription factor Y subunit alpha
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P23511-2
-
Expression Region
1-318aa
-
AA Sequence
MEQYTANSNSSTEQIVVQAGQIQQQVQGQPLMVQVSGGQLITSTGQPIMV QAVPGGQGQTIMQVPVSGTQGLQQIQLVPPGQIQIQGGQAVQVQGQQGQT QQIIIQQPQTAVTAGQTQTQQQIAVQGQQVAQTAEGQTIVYQPVNADGTI LQQVTVPVSGMITIPAASLAGAQIVQTGANTNTTSSGQGTVTVTLPVAGN VVNSGGMVMMVPGAGSVPAIQRIPLPGAEMLEEEPLYVNAKQYNRILKRR QARAKLEAEGKIPKERRKYLHESRHRHAMARKRGEGGRFFSPKEKDSPHM QDPNQADEEAMTQIIRVS
-
Molecular Weight
34 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
NFYA (Nuclear Factor Y Subunit A) is a pivotal transcription factor involved in various biological processes, including cell cycle regulation, stress response, and development. The NFYA protein is part of a larger complex, NFY, which typically binds to CCAAT motifs in gene promoters, influencing the transcription of genes critical for growth and metabolism. Research has highlighted NFYA's role in cancer biology, where its dysregulation is often linked to tumor progression and poor prognosis. Additionally, NFYA is implicated in various stress responses, including heat and oxidative stress, showcasing its potential as a therapeutic target. The reconstitution of NFYA as a recombinant protein provides a powerful tool for elucidating its functional dynamics, interaction with DNA, and downstream effects on gene expression. Studies utilizing recombinant NFYA can lead to advancements in understanding its structural properties, post-translational modifications, and the mechanism of its action in both normal and pathological states. This research is essential for developing targeted therapies that can modulate NFYA's activity, restoring normal function in diseased tissues and enhancing our understanding of gene regulation mechanisms in cellular responses. The exploration of NFYA’s role in different contexts, such as aging and chronic diseases, further emphasizes the need for detailed structural and functional studies of this protein. By investigating NFYA through the lens of recombinant technology, scientists aim to uncover novel insights that could pave the way for innovative medical interventions.











