Recombinant TBC1D4 Monoclonal Antibody (AN300720L)
For research use only.
| Verified Samples | Verified Samples in WB: HepG2 |
| Dilution | WB 1:2000-1:10000, |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human TBC1D4 protein |
| Abbre | TBC1D4 |
| Synonyms | KIAA, NIDDM, TBC1D, AS160, NIDDM5, TBC1D4, KIAA0603, Acrg embryonic lethality (mouse) minimal region ortholog, Acrg embryonic lethality minimal region ortholog, Acrg embryonic lethality mouse minimal region ortholog, Akt substrate of 160 kDa, AS 160, BUB2, CDC16, TBC (Tre 2 BUB2 CDC16) domain containing protein, TBC Tre 2 BUB2 CDC16 domain containing protein, TBC1 D4, TBC1 domain family member 4, TBCD4, Tre-2 |
| Swissprot | |
| Calculated MW | 147 kDa |
| Observed MW |
160 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 |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Signal Transduction |
| Clone No. | 11A2 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene is a member of the Tre-2/BUB2/CDC16 domain family. The protein encoded by this gene is a Rab-GTPase-activating protein, and contains two phopshotyrosine-binding domains (PTB1 and PTB2), a calmodulin-binding domain (CBD), a Rab-GTPase domain, and multiple AKT phosphomotifs. This protein is thought to play an important role in glucose homeostasis by regulating the insulin-dependent trafficking of the glucose transporter 4 (GLUT4), important for removing glucose from the bloodstream into skeletal muscle and fat tissues. Reduced expression of this gene results in an increase in GLUT4 levels at the plasma membrane, suggesting that this protein is important in intracellular retention of GLUT4 under basal conditions. When exposed to insulin, this protein is phosphorylated, dissociates from GLUT4 vesicles, resulting in increased GLUT4 at the cell surface, and enhanced glucose transport. |
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Unconjugated
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