Recombinant Human Hsp27

Recombinant Human Hsp27

• Description: Recombinant Human Hsp27
• Product Name Alternative: Hsp27
• CAS Number: 9000-83-3
• Gene Name: HSPB1
• UniProt: P04792
• Cellular Locus: Cytoplasm , Nucleus , Cytoplasm, cytoskeleton, spindle , Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
• Reactivity: Human
• Target Antigen: Heat shock protein beta-1
• Target: Hsp27
• Type: Protein
• Applications: WB
• Concentration: Lot Specific
• Dilution: Dilute in PBS or medium that is identical to that used in the assay system.
• Form: Liquid
• Buffer: 20mM HEPES, 1mM DTT, and 100mM KCl.
• Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742). {PubMed:10383393, PubMed:19166925, PubMed:20178975, PubMed:23728742}.
• Storage Conditions: Although stable at 4°C for 1 week, product is best stored at or below -20°C. Addition of a carrier protein (such as 0.1% HSA or BSA) is recommended for long-term storage.
• Specificity: Hsp27
• Formulation: Sterile-filtered colorless solution in 20mM HEPES, pH 7.5, 1mM DTT, and 100mM KCl.
• Buffer pH: pH 7.5
• Target Background: Hsp27, a mammalian heat shock protein, is expressed constitutively in many tissues, and its expression level increases in response to various stress conditions including elevated temperatures, toxic metals, drugs, and oxidants. Hsp27 is phosphorylated in vivo at three phosphorylation sites (Ser15, Ser78, and Ser82) by protein kinases including MAPKAP kinase 2 and stress-activated protein kinase SAPK2.