Recombinant HSP27/HSPB1 Monoclonal Antibody (AN300325P)

For research use only.
Verified Samples |
Verified Samples in IF: A431, SKBR3 Verified Samples in FCM: HeLa |
Dilution | ICC/IF 1:20-1:100, FCM 1:25-1:100 |
Isotype | IgG |
Host | Rabbit |
Reactivity | Human |
Applications | FCM, ICC/IF |
Clonality | Monoclonal |
Immunogen | Recombinant Human HSP27 protein |
Abbre | HSPB1 |
Synonyms | SRP, HSPB, HEL-S, HSP, HSPB1, CMT2F, HEL-S-102, HMN2B, HS.76067, HSP27, HSP28, Hsp25, SRP27, 28 kDa heat shock protein, DKFZp586P1322, epididymis secretory protein Li 102, Estrogen regulated 24 kDa protein, Estrogen-regulated 24 kDa protein, Heat shock 25kDa protein 1, Heat shock 27 kDa protein, Heat shock 27kD protein 1, Heat shock 27kDa protein, Heat shock 27kDa protein 1, Heat shock 28kDa protein 1, Heat Shock Protein 27, Heat shock protein beta 1, Heat shock protein beta-1, heat shock protein family B (small) member 1, Hsp 25, HSP 27, Hsp 28, Hsp B1, Stress responsive protein 27, Stress-responsive protein 27 |
Swissprot | |
Cellular Localization | Cytoplasm,Nucleus,Cytoplasm, cytoskeleton, spindle |
Tissue Specificity | Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle. |
Concentration | 1 mg/mL |
Buffer | 0.2 μm filtered solution in PBS |
Purification Method | Protein A |
Research Areas | Signal Transduction, Cancer, Cardiovascular |
Clone No. | 9F4 |
Conjugation | Unconjugated |
Storage | This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles. |
Shipping | Ice bag |
background | The heat shock proteins are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. Some HSPs are expressed at low levels under normal physiological conditions but show dramatically increased expression in response to cellular stress, others are constitutively expressed. Specific HSPs play a role in regulating apoptosis by interacting directly with key components of the apoptotic pathway. |
Other Clones
{{antibodyDetailsPage.numTotal}} Results
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.:{{item.cat}}
{{index}} {{goods_show_value}}
Other Formats
{{formatDetailsPage.numTotal}} Results
Unconjugated
-
{{item.title}}
Citations ({{item.publications_count}}) Manual MSDS
Cat.No.:{{item.cat}}
{{index}} {{goods_show_value}}
-
IF:{{item.impact}}
Journal:{{item.journal}} ({{item.year}})
DOI:{{item.doi}}Reactivity:{{item.species}}
Sample Type:{{item.organization}}
-
Q{{(FAQpage.currentPage - 1)*pageSize+index+1}}:{{item.name}}
