Recombinant Cpn10 Monoclonal Antibody (AN301498L)
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For research use only.
| Verified Samples |
Verified Samples in WB: MCF-7, 293, 4T1, PC-12 Verified Samples in IHC: Human colon, Rat colon Verified Samples in IF: HeLa |
| Dilution | WB 1:500-1:1000, IHC 1:200-1:1000, IF 1:50 |
| Isotype | IgG, κ |
| Host | Rabbit |
| Reactivity | Human, Rat, Mouse |
| Applications | WB, IHC, IF |
| Clonality | Monoclonal;Recombinant |
| Immunogen | Recombinant human Cpn10 fragment |
| Abbre | Cpn10 |
| Synonyms | CPN, HSP, HSPE, HSPE1, CPN10, EPF, GROES, HSP10, 10 kDa chaperonin, 10 kDa heat shock protein, 10 kDa heat shock protein mitochondrial, CH10, Chaperonin 10, Chaperonin 10 homolog, cpn10 homolog, Early pregnancy factor, Early-pregnancy factor, GroES homolog, Heat shock 10kD protein 1 chaperonin 10, Heat shock 10kDa protein 1, Heat shock 10kDa protein 1 chaperonin 10, Heat shock protein family E (Hsp10) member, Heat-shock 10-kD protein, mitochondrial |
| Swissprot | |
| Calculated MW | 11 kDa |
| Observed MW |
11 kDa
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 | Mitochondrion |
| 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, Metabolism |
| Clone No. | A193 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. |
Other Clones
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Unconjugated
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