MTHFD1 Antibody | 23-700

MTHFD1 Antibody | 23-700 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human, Mouse, Rat

Homology: N/A

Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 1-270 of human MTHFD1 (NP_005947.3) .

Research Area: Cancer, Cell Cycle, Signal Transduction

Tested Application: WB

Application: WB: 1:200 - 1:2000

Specificiy: N/A

Positive Control 1: Raji

Positive Control 2: LO2

Positive Control 3: Mouse brain

Positive Control 4: Mouse kidney

Positive Control 5: Rat spinal cord

Positive Control 6: N/A

Molecular Weight: Observed: 115kDa

Validation: N/A

Isoform: N/A

Purification: Affinity purification

Clonality: Polyclonal

Clone: N/A

Isotype: IgG

Conjugate: Unconjugated

Physical State: Liquid

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Concentration: N/A

Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.

Alternate Name: MTHFD1, methylenetetrahydrofolate dehydrogenase (NADP+ dependent) 1, methenyltetrahydrofolate cyclohydrolase, formyltetrahydrofolate synthetase, MTHFC, MTHFD, 5, 10-methylenetetrahydrofolate dehydrogenase, 10-methylenetetrahydrofolate cyclohydrolase, 10-formyltetrahydrofolate synthetase, C1-THF synthase, NADP-dependent cyclohydrolase/formyltetrahydrofolate synthetase, cytoplasmic C-1-tetrahydrofolate synthase, methylenetetrahydrofolate dehydrogenase (NADP+ dependent) , methylenetetrahydrofolate dehydrogenase 1

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

BACKGROUND: This gene encodes a protein that possesses three distinct enzymatic activities, 5, 10-methylenetetrahydrofolate dehydrogenase, 5, 10-methenyltetrahydrofolate cyclohydrolase and 10-formyltetrahydrofolate synthetase. Each of these activities catalyzes one of three sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses. The trifunctional enzymatic activities are conferred by two major domains, an aminoterminal portion containing the dehydrogenase and cyclohydrolase activities and a larger synthetase domain.