HSP-60 Polyclonal Antibody (AN005850L)
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For research use only.
| Verified Samples |
Verified Samples in WB: HeLa, Mouse heart, Rat brain, Rat heart, Rat spleen, Rat liver Verified Samples in IHC: Human liver Verified Samples in IF: HeLa, NIH/3T3, C6 |
| Dilution | WB 1:1000-1:2000, IHC 1:400-1:800, IF 1:200-1:400 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB, IHC, IF |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human HSP-60 protein expressed by E.coli |
| Abbre | HSP-60 |
| Synonyms | 60 kDa heat shock protein, 60-KD, CH60, fa04a05, heat shock 60kDa protein 1 (chaperonin), Heat shock protein 1 (chaperonin), Heat shock protein 60, Heat shock protein 65, heat shock protein family D (Hsp60) member 1, Hsp 60, HSP 65, mitochondrial, Mitochondrial matrix protein P1, P60 lymphocyte protein, short heat shock protein 60 Hsp60s1, HLD, SPG, CPN, Chaperonin, HSPD, HuCHA, GROEL, HLD4, HSP-60, HSP65, HuCHA60, SPG13, CPN60, Mitochond, 60 kDa chaperonin, Chaperonin 60, HSP60, HSPD1 |
| Swissprot | |
| Calculated MW | 61 kDa |
| Observed MW |
60 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 | Mitochondrion |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Research Areas | Tags & Cell Markers, Signal Transduction, Kits, Lysates, Other, Isotype, Loading Controls |
| 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 | Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically upregulated in response to cellular stress. Heat Shock Protein 60 (HSP60), also known as Chaperonin 60 (CPN60), is a mitochondrial matrix protein belonging to a highly conserved family of molecular chaperone and stress response proteins. HSP60 plays a role in stabilizing and refolding proteins in response to heat-shock or other cellular stress. Full length human HSP60 is 98% identical to mouse and rat HSP60. |
Other Clones
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Other Formats
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Unconjugated
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