Recombinant Bag3 Monoclonal Antibody (AN300926L)
For research use only.
| Verified Samples | Verified Samples in WB: HEK293 |
| Dilution | WB 1:1000-1:5000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant Human Bag3 protein |
| Abbre | Bag3 |
| Synonyms | MFM, CAIR, Bcl-2-associated athanogene, BAG family molecular chaperone regulator, BAG, BAG3, BAG-3, BIS, CAIR-1, MFM6, BAG family molecular chaperone regulator 3, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, Bcl-2-associated athanogene 3, Bcl-2-binding protein Bis, BIS, BAG 3, BAG family molecular chaperone regulator 3, Bcl 2 binding protein, BCL2 associated athanogene 3, BCL2 binding athanogene 3, CAIR 1, Docking protein CAIR 1, Docking protein CAIR-1, Bag-3 |
| Swissprot | |
| Calculated MW | 62 kDa |
| Observed MW |
80 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, Nucleus |
| Tissue Specificity | Brain, skeletal muscle |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Cell Biology, Cancer, Metabolism |
| Clone No. | 8A1 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. |
Other Clones
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Unconjugated
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