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HSP27 monoclonal antibody (G3.1) (DyLight™ 488 conjugate)

 
ADI-SPA-800-488-E 100 µg 334.00 USD
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Product Specification

Alternative Name:HspB1, Heat shock protein 27
 
Clone:G3.1
 
Host:Mouse
 
Isotype:IgG1
 
Immunogen:Native human Hsp27.
 
UniProt ID:P04792
 
GenBank ID:L39370
 
Species reactivity:Human, Mouse, Rat
Bovine, Fish, Monkey
 
Applications:Flow Cytometry
 
Recommended Dilutions/Conditions:Flow Cytometry (50µg/ml)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Purity Detail:Protein G affinity purified.
 
Formulation:Liquid. In PBS, pH 7.2, containing 0.09% sodium azide.
 
Handling:Avoid freeze/thaw cycles. Protect from light.
 
Shipping:Blue Ice Not Frozen
 
Long Term Storage:+4°C
 
Scientific Background:Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
 
ADI-SPA-800-488 FC
Flow cytometry analysis of 105 HeLa cells stained using HSP27 mAb (G3.1) , DyLight™ 488 conjugate at a concentration of 50µg/mL.
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ADI-SPA-800-488 FC

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Heat Shock Proteins & the Cellular Stress Response Catalog
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