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For research use only.

Verified Samples Verified Samples in WB: 293T, HepG2, Hela
Verified Samples in IHC: Human uterus
Verified Samples in IF: Human liver cancer
Dilution WB 1:500-1:3000,  IHC 1:50-300,  IF 1:100-1:300
Isotype IgG
Host Mouse
Reactivity Human,  Mouse,  Rat
Applications WB,  IHC-p,  IF
Clonality Monoclonal
Immunogen Synthetic Peptide
Abbre FH
Synonyms FH,  FUMH,  Fumarase,  Fumarate hydratase,  Fumarate hydratase mitochondrial,  HLRCC,  LRCC,  MCL,  MCUL 1,  MCUL1,  MS709,  Multiple hereditary cutaneous leiomyomata,  mitochondrial
Swissprot
Observed MW 50 kDa
The actual band is not consistent with the expectation.

Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include:

1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein.

2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes.

3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1.

4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids).

5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers.

If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane.

Cellular Localization Cytoplasm and Mitochondrion.
Tissue Specificity Expressed in red blood cells, underexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.
Concentration 1 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol.
Purification Method Protein A purification
Research Areas Cancer,  Metabolism,  Signal Transduction
Clone No. 5H2
Conjugation Unconjugated
Storage Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles.
Shipping The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended.
background The protein encoded by this gene is an enzymatic component of the tricarboxylic acid (TCA) cycle, or Krebs cycle, and catalyzes the formation of L-malate from fumarate. It exists in both a cytosolic form and an N-terminal extended form, differing only in the translation start site used. The N-terminal extended form is targeted to the mitochondrion, where the removal of the extension generates the same form as in the cytoplasm. It is similar to some thermostable class II fumarases and functions as a homotetramer. Mutations in this gene can cause fumarase deficiency and lead to progressive encephalopathy.
Other Clones

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Other Formats

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Unconjugated

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