HSP27/HSPB1 Protein, Human (His)

The HSP27/HSPB1 protein is a small heat shock protein that acts as a molecular chaperone, possibly maintaining denatured proteins in a foldable state. In addition to its chaperone role, it crucially enhances stress resistance and contributes to actin organization. HSP27/HSPB1 Protein, Human (His) is the recombinant human-derived HSP27/HSPB1 protein, expressed by E. coli , with C-His labeled tag. The total length of HSP27/HSPB1 Protein, Human (His) is 205 a.a..

HSP27/HSPB1, a small heat shock protein, serves as a molecular chaperone with a likely role in maintaining denatured proteins in a folding-competent state. Beyond its chaperone function, this protein plays a crucial role in stress resistance and contributes to actin organization. Its molecular chaperone activity is implicated in regulating various biological processes, including the phosphorylation and axonal transport of neurofilament proteins. HSP27/HSPB1 forms homooligomers and homodimers, the latter transitioning to a monomeric state upon activation. Additionally, it participates in heterooligomer formation with HSPB6. The protein interacts with alpha- and beta-tubulin, and it engages in molecular associations with TGFB1I1, CRYAB, HSPB8, and HSPBAP1, thereby contributing to a network of protein-protein interactions that underlie its diverse cellular functions.

Human

E. coli

C-His

P04792/NP_001531.1 (M1-K205)

3315  [NCBI]

MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK

Approximately 26-28 kDa

Greater than 95% as determined by reducing SDS-PAGE

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 20 mM HEPES, 0.1M KCl, pH 7.5 or PBS, pH 7.4, 8% trehalose.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.