NFYA Antibody | 27-329

NFYA Antibody | 27-329 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat, Dog

Homology: N/A

Immunogen: Antibody produced in rabbits immunized with a synthetic peptide corresponding a region of human NFYA.

Research Area: Transcription, Cancer

Tested Application: E, WB, IHC

Application: NFYA antibody can be used for detection of NFYA by ELISA at 1:62500. NFYA antibody can be used for detection of NFYA by western blot at 0.2-2.0 μg/mL, and HRP conjugated secondary antibody should be diluted 1:50, 000 - 100, 000.

Specificiy: N/A

Positive Control 1: Cat. No. 1205 - Jurkat Cell Lysate

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 37 kDa, 34 kDa

Validation: N/A

Isoform: N/A

Purification: Antibody is purified by peptide affinity chromatography method.

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Concentration: batch dependent

Storage Condition: For short periods of storage (days) store at 4˚C. For longer periods of storage, store NFYA antibody at -20˚C. As with any antibody avoid repeat freeze-thaw cycles.

Alternate Name: NFYA, HAP2, CBF-A, CBF-B, NF-YA

User Note: Optimal dilutions for each application to be determined by the researcher.

BACKGROUND: NFYA is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.