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For research use only.

Verified Samples Verified Samples in WB: Human fetal muscle, HepG2, Jurkat, Hela, A431, A549
Verified Samples in IHC: Human tonsil, Human esophagus cancer
Dilution WB 1:500-1:2000,  IHC 1:30-1:150
Isotype IgG
Host Rabbit
Reactivity Human
Applications WB,  IHC
Clonality Polyclonal
Immunogen Synthetic peptide of human BAG2
Abbre BAG2
Synonyms BAG 2,  BAG family molecular chaperone regulator 2,  BAG-2,  BAG-family molecular chaperone regulator-2,  BAG2,  BCL 2 associated athanogene 2,  BCL2 associated athanogene 2,  BCL2-associated athanogene 2,  Bag2,  Bcl-2-associated athanogene 2,  dJ417I1.2 (BAG family molecul
Swissprot
Calculated MW 24 kDa
Observed MW Refer to figures
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 Cytoskeleton, Cytoplasm.
Concentration 0.9 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer and 50% glycerol.
Purification Method Antigen affinity purification
Research Areas Cell Biology,  Signal Transduction,  Cancer,  Metabolism
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 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 predicted BAG2 protein contains 211 amino acids. 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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