Recombinant Alpha B Crystallin Monoclonal Antibody (AN301434L)
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For research use only.
| Verified Samples |
Verified Samples in WB: Rat eyes, Mouse eyes Verified Samples in IHC: Human cerebellum, Human cerebrum, Mouse cerebrum, Mouse kidney, Rat cerebrum, Rat kidney |
| Dilution | WB 1:500-1:2000, IHC 1:200-1:1000 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB, IHC |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Alpha B Crystallin fragment |
| Abbre | Alpha B Crystallin |
| Synonyms | MFM, CRYA, CTPP, HSPB, Heat Shock Protein Beta, Renal Carcinoma Antigen NY-REN, CTRCT, HEL-S, CRYAB, CMD1II, CRYA2, CTPP2, CTRCT16, HEL-S-101, HSPB5, MFM2, Alpha(B)-Crystallin, Alpha-Crystallin B Chain, Heat Shock Protein Beta-5, Renal Carcinoma Antigen NY-REN-27, Rosenthal Fiber Component, AACRYA, Alpha B crystallin, Alpha crystallin B chain, Crystallin alpha B, Crystallin alpha polypeptide 2, Heat shock 20 kD like protein, Heat shock protein beta 5, Renal carcinoma antigen NY REN 27 |
| Swissprot | |
| Calculated MW | 20 kDa |
| Observed MW |
22 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, Secreted |
| Concentration | 1 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A purified |
| Research Areas | Signal Transduction, Neuroscience, Cancer, Metabolism |
| Clone No. | A129 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. |
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