HSP27 recombinant protein

HSP27, 1-205aa, Human, His tag, E Coli

Cat. Num. AAA203631

• Gene Names: HSPB1; CMT2F; HMN2B; HSP27; HSP28; Hsp25; SRP27; HS.76067; HEL-S-102
• Applications: SDS-Page
• Purity: > 95% by SDS-PAGE
• Synonyms: HSP27; 1-205aa; Human; His tag; E Coli; Heat shock protein beta-1; CMT2F; HMN2B; Hsp25; HSP27 recombinant protein

• Host: E Coli
• Purity/Purification: > 95% by SDS-PAGE
• Form/Format: Liquid. In 20mM Tris-HCl Buffer (pH 8.0) containing 10% glycerol, 1mM DTT, 0.1 M NaCl.
• Concentration: 1 mg/ml (determined by Bradford assay) (varies by lot)
• Sequence: MGSSHHHHHH SSGLVPRGSH MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK
• Sequence Length: 205

• Applicable Applications for HSP27 recombinant protein: SDS-PAGE
• Antigen Species: Human
• Tag Information: His-tag
• Endotoxin Level: < 1.0 EU per 1 microgram of protein (determined by LAL method)
• Preparation and Storage: Can be stored at 4 degree C short term (1-2 weeks).; For long term storage, aliquot and store at -20 degree C or -70 degree C.; Avoid repeated freezing and thawing cycles.

SDS-Page

Related Product Information for HSP27 recombinant protein

Hsp27 (also known as the Estrogen-Regulated 24K protein, and hsp 28) is a member of the mammalian small heat shock protein family. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants. Also, Hsp27 is phosphorylated in vivo on three phosphorylation sites (Ser15, Ser78 and Ser82) by protein kinases including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38). Recombinant human HSP27 protein, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.

Product Categories/Family for HSP27 recombinant protein

Heat Shock Proteins

References

Friedman MJ., et al. (2009) J Biol Chem. 284 (41):27944-51. ; Brunet Simioni M., et al. (2009) Oncogene. 28 (37):3332-44.;

NCBI and Uniprot Product Information

• NCBI GI #: 4504517
• NCBI GeneID: 3315
• NCBI Accession #: NP_001531
• NCBI GenBank Nucleotide #: NM_001540.4
• UniProt Accession #: P04792; Q6FI47; Q96C20; Q96EI7; Q9UC31; Q9UC34; Q9UC35; Q9UC36; B2R4N8
• Molecular Weight: 24.9 kDa (225aa), confirmed by MALDI-TOF.
• NCBI Official Full Name: heat shock protein beta-1
• NCBI Official Synonym Full Names: heat shock protein family B (small) member 1
• NCBI Official Symbol: HSPB1
• NCBI Official Synonym Symbols: CMT2F; HMN2B; HSP27; HSP28; Hsp25; SRP27; HS.76067; HEL-S-102
• NCBI Protein Information: heat shock protein beta-1
• UniProt Protein Name: Heat shock protein beta-1
• Protein Family: Heat shock protein
• UniProt Gene Name: HSPB1
• UniProt Synonym Gene Names: HSP27; HSP28; HspB1; HSP 27; SRP27

NCBI Description

This gene encodes a member of the small heat shock protein (HSP20) family of proteins. In response to environmental stress, the encoded protein translocates from the cytoplasm to the nucleus and functions as a molecular chaperone that promotes the correct folding of other proteins. This protein plays an important role in the differentiation of a wide variety of cell types. Expression of this gene is correlated with poor clinical outcome in multiple human cancers, and the encoded protein may promote cancer cell proliferation and metastasis, while protecting cancer cells from apoptosis. Mutations in this gene have been identified in human patients with Charcot-Marie-Tooth disease and distal hereditary motor neuropathy. [provided by RefSeq, Aug 2017]

Uniprot Description

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).