Hsp27 Antibody
- 貨號 Cat. No.
- 3092-100
- 規格 Size
- 100 µg
Description
pstrongAntibody Target :/strongHsp27/p
pbHost: /bRabbit/p
pbAntibody Type: /bPolyclonal/p
pbIsotype: /bRabbit IgG/p
pbAntibody Form: /bAffinity Purified Antibody/p
pbImmunogen Sequence: /bRecombinant human Hsp27/p
pbAccession#: /bBAB17232/p
pbGene ID: /b11036357/p
pbAppearance: /bColorless liquid/p
pbConcentration: /b0.2 mg/ml/p
pbFormulation: /b100 micro;g (200 micro;g/ml) in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA, 0.02% thimerosal./p
pbPurification: /bAffinity purified/p
pbSpecies Reactivity: /bhu/mk/p
pbApplication: /bWB/IP/IF/p
pbApplication amp; Usage: /bWestern blotting (1-2 micro;g/ml), immunoprecipitation (5-10 micro;g/ml), immunocytochemistry (10-15 micro;g/ml), and ELISA (1 micro;g/ml). However, the optimal conditions should be determined individually. The antibody detects a 27 kDa protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, dog (weakly) and pig (weakly) origins./p
pbStorage Temp.: /b-20 deg;C/p
pbShipping : /bgel pack/p
pbShelf Life: /b12 months/p
pbHandling: /bThe antibody solution should be gently mixed before use./p
pbBrief Background Descriptions: /bHuman Hsp27, mouse Hsp25 and alpha;beta;-crystallin are part of a diverse family of small heat shock proteins which are produced in all organisms. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. Hsp27 is believed to exist mainly as oligomers of as many as 8-40 Hsp27 protein monomers in cells and data suggests that the large oligomers of Hsp27 have a chaperone-like activity by serving as a site where unfolding proteins may bind until ATP and Hsp70-dependent refolding can occur. Hsp27 is believed to protect cells by enhancing cellular glutathione levels and elevated glutathione levels have been measured in cells overexpressing Hsp27. Data from studies using wild-type Hsp27 and mutant forms in which the serine phosphorylation sites were mutated to alanines, glycines or aspartates, have shown that cellular glutathione levels depend on the oligomerization of Hsp27. Recent findings indicate that Hsp27 is also a negative regulator of cytochrome c-dependent activation of procaspase-3./p
pbHost: /bRabbit/p
pbAntibody Type: /bPolyclonal/p
pbIsotype: /bRabbit IgG/p
pbAntibody Form: /bAffinity Purified Antibody/p
pbImmunogen Sequence: /bRecombinant human Hsp27/p
pbAccession#: /bBAB17232/p
pbGene ID: /b11036357/p
pbAppearance: /bColorless liquid/p
pbConcentration: /b0.2 mg/ml/p
pbFormulation: /b100 micro;g (200 micro;g/ml) in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA, 0.02% thimerosal./p
pbPurification: /bAffinity purified/p
pbSpecies Reactivity: /bhu/mk/p
pbApplication: /bWB/IP/IF/p
pbApplication amp; Usage: /bWestern blotting (1-2 micro;g/ml), immunoprecipitation (5-10 micro;g/ml), immunocytochemistry (10-15 micro;g/ml), and ELISA (1 micro;g/ml). However, the optimal conditions should be determined individually. The antibody detects a 27 kDa protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, dog (weakly) and pig (weakly) origins./p
pbStorage Temp.: /b-20 deg;C/p
pbShipping : /bgel pack/p
pbShelf Life: /b12 months/p
pbHandling: /bThe antibody solution should be gently mixed before use./p
pbBrief Background Descriptions: /bHuman Hsp27, mouse Hsp25 and alpha;beta;-crystallin are part of a diverse family of small heat shock proteins which are produced in all organisms. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. Hsp27 is believed to exist mainly as oligomers of as many as 8-40 Hsp27 protein monomers in cells and data suggests that the large oligomers of Hsp27 have a chaperone-like activity by serving as a site where unfolding proteins may bind until ATP and Hsp70-dependent refolding can occur. Hsp27 is believed to protect cells by enhancing cellular glutathione levels and elevated glutathione levels have been measured in cells overexpressing Hsp27. Data from studies using wild-type Hsp27 and mutant forms in which the serine phosphorylation sites were mutated to alanines, glycines or aspartates, have shown that cellular glutathione levels depend on the oligomerization of Hsp27. Recent findings indicate that Hsp27 is also a negative regulator of cytochrome c-dependent activation of procaspase-3./p