Recombinant Human Hsp27/HSPB1-Protein
Beta LifeScience
SKU/CAT #: BLK-00304P-100UG

Human Hsp27 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.
Recombinant Human Hsp27/HSPB1-Protein
Beta LifeScience
SKU/CAT #: BLK-00304P-100UG
Collections: High-quality recombinant proteins, Other recombinant proteins
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.
Product Overview
Description | Recombinant Human Hsp27/HSPB1-Protein is expressed from E.coli with His tag at the C-Terminus.It contains Met1-Lys205. |
Purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
Accession | NP_001531.1 |
Target Symbol | Hsp27/HSPB1 |
Species | Human |
Expression System | E. coli |
Tag | C-His |
Expression Range | Met1-Lys205 |
Mol. Weight | The protein has a predicted MW of 23.74 kDa. The protein migrates to 25-30 kDa based on Tris-Bis PAGE result. |
Form | Lyophilized |
Formulation | Lyophilized from 0.22um filtered solution in PBS, 2mM DTT (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization. |
Endotoxin | Less than 1EU per ug by the LAL method. |
Storage | Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. |
Shipping | Shipped at ambient temperature. |
Gene Background | Heat shock protein beta-1 (HSPB1, also known as HSP27) is a small heat shock protein involved in many cellular processes and reportedly protects cells against oxidative stress. This protein is expressed only in insulin-dependent tissues (heart, skeletal muscle, and fat tissue), and expression of HspB7 is regulated by many different factors. HspB7 has an unusual N-terminal sequence, a conservative α-crystallin domain, and very short C-terminal domain lacking conservative IPV tripeptide involved in a small heat shock proteins oligomer formation. |