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Hsp27 (human recombinant)

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    Hsp27 (human recombinant)
  • Hsp27 (human recombinant)
Cat No: 22736
Proteins - Enzymes
Cayman
€263.00
Price is excluding VAT and does not include packaging neither shipping

Heat shock protein 27 (Hsp27), also known as heat shock protein beta-1 (HspB1), is a member of the small heat shock protein (sHSP) family that is upregulated during conditions of cellular stress including heat shock, radiation, hypoxia, and exposure t...

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: 50 µg

This product can only be bought through Cayman Chemical. Please contact us.

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Territorial Availability: Available through Bertin Pharma only in Europe
Correlated keywords:
  • Estrogen-regulated 24K Beta1 28 kDa HSP28 Hsp25 CMT2F HspB1 SRP27 P Anastasis
Product Overview:
Heat shock protein 27 (Hsp27), also known as heat shock protein beta-1 (HspB1), is a member of the small heat shock protein (sHSP) family that is upregulated during conditions of cellular stress including heat shock, radiation, hypoxia, and exposure to reactive oxygen species (ROS).{40293,40294} It is composed of an N-terminal domain, a highly conserved alpha-crystallin domain, and a C-terminal domain. Hsp27 functions as a molecular chaperone to prevent protein aggregation in an ATPase-independent manner. This chaperone activity is altered by changes in oligomerization state or by post-translational modifications including phosphorylation at serine residues 15 and 82, which increases affinity for damaged polypeptides in response to heat shock.{40754} Hsp27 also works in complex with other chaperone proteins, such as Hsp70 (Item Nos. 22739
23002), to correct misfolded proteins. This protein also plays a role in apoptosis, proteasome activation, cell differentiation, and has been shown to interact with actin and intermediate filaments.{40295,40296,40297} Mutations in HSPB1 have been linked to hereditary neuromuscular diseases and cause Charcot-Marie-Tooth Disease Type 2 (CMT-2).{40298}
Size 50 µg
Shipping dry ice
Stability Store at -80 degrees; shelf life 365 days
Purity ≥90% as estimated by SDS-PAGE
Custom Code 3504.00
UNSPSC code 12352204

Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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