Hsp27 (11110P-10)
| Host | Quantity | Applications | Species Reactivity | Data Sheet | |
|---|---|---|---|---|---|
| 10ug | WB | Human |  |
Overview
Product Name Hsp27 (11110P-10)
Description Recombinant human Hsp-27 produced in E. coli is a single, non-glycosylated polypeptide containing 205 amino acids with a molecular weight of 22.7kDa.
Target Hsp27
Species Reactivity Human
Applications WB
Source Escherichia coli
Properties
Form Liquid
Concentration Lot Specific
Formulation Sterile-filtered colorless solution in 20mM HEPES, pH 7.5, 1mM DTT, and 100mM KCl.
Buffer Formulation 20mM HEPES, 1mM DTT, and 100mM KCl.
Buffer pH pH 7.5
Purity Greater than 95% as determined by SDS-PAGE and RP- HPLC
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.
Specificity Information
Target Name Heat shock protein beta-1
Target ID Hsp27
Alternative Names Hsp27
Sequence Location 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.
Sequence MTERRVPFSLLRGPSWDPFR DWYPHSRLFDQAFGLPRLPE EWSQWLGGSSWPGYVRPLPP AAIESPAVAAPAYSRALSRQ LSSGVSEIRHTADRWRVSLD VNHFAPDELTVKTKDGVVEI TGKHEERQDEHGYISRCFTR KYTLPPGVDPTQVSSSLSPE GTLTVEAPMPKLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK
Biological 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}.
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.
Handling
Storage 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.
Dilution Instructions Dilute in PBS or medium that is identical to that used in the assay system.
References & Data Sheet
Data Sheet 
Download PDF Data Sheet
Download PDF Data Sheet