Description
MTHFD1 Antibody | 61-504 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human
Homology: Predicted species reactivity based on immunogen sequence: Mouse, Rat
Immunogen: This MTHFD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 535-562 amino acids from the Central region of human MTHFD1.
Research Area: Cell Cycle, Obesity, Signal Transduction
Tested Application: WB, IHC-P, IF
Application: For WB starting dilution is: 1:1000
For IF starting dilution is: 1:10~50
For IHC-P starting dilution is: 1:50~100
Specificiy: N/A
Positive Control 1: N/A
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: 102 kDa
Validation: N/A
Isoform: N/A
Purification: This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis
Clonality: Polyclonal
Clone: N/A
Isotype: Rabbit Ig
Conjugate: Unconjugated
Physical State: Liquid
Buffer: Supplied in PBS with 0.09% (W/V) sodium azide.
Concentration: batch dependent
Storage Condition: Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.
Alternate Name: C-1-tetrahydrofolate synthase, cytoplasmic, C1-THF synthase, Methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, Formyltetrahydrofolate synthetase, C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed, MTHFD1, MTHFC, MTHFD
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: MTHFD1 is 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.