商品编号


YIF-LF-P0321



品牌


Adipogen



公司


Adipogen



公司分类


Proteins



Size

0.2 mg

商品信息


More Information



Product Details



Synonyms

HSPB1; HspB1; HSP27; SRP27; HSP 27; Heat Shock 27 kDa Protein; 28 kDa Heat Shock Protein; Heat Shock Protein β-1; Stress-responsive Protein 27; Estrogen-regulated 24 kDa Protein



Product Type

Protein



Properties



Source/Host

E. coli



Crossreactivity

Human



Purity

≥95% (SDS-PAGE)



Formulation

Lyophilized from 50mM NaH2PO4, pH8.0 / 300mM NaCl / 250mM imidazole.



Other Product Data

Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.



Declaration

Manufactured by AbFrontier



Shipping and Handling



Shipping

BLUE ICE



Short Term Storage

+4°C



Long Term Storage

-20°C



Handling Advice

Avoid freeze/thaw cycles.



Use/St
ABI
lity

After reconstitution, store at -80°C.



Documents



MSD
S

No



Product Specification Sheet



Datasheet


Download PDF





Heat shock proteins are ubiquitous proteins and have been characterized as cytoprotective molecular chaperones. The typical function of a chaperone is to assist a protein to attain its functional conformation to prevent non-functional aggregation of misfolded proteins. The principal HSP families are HSP90, HSP70, HSP60 and the small HSPs including HSP27, ubiquitin, α-crystallin, Hsp20 and others. The common functions of small Hsps are chaperone activity,
Thermo
tolerance, inhibition of apoptosis, regulation of cell development, and cell differentiation. Hsp27 has a molecular weight of approximately 27 kDa, although it has been shown to form large aggregates of up to 800 kDa in the cytosol. Hsp27 is found in several types of human cells, including tumour cells. Hsp27 interferes with apoptosis through its
ABI
lity to interact with and inhibit key components of the apoptotic signaling pathway, including the caspase activation complex. Overexpression of heat shock proteins can increase the tum
Origen
ic potential of tumour cells. HSP27 also has been reported to be involved in development and progression of hormone-refractory prostate cancer.


Product References
1) So A et al., (2007) Curr Genomics 8(4):252-261. (General)
2) Ferns G et al., (2006) Int J Exp Pathol 87(4):253-274. (General)
3) Ciocca DR and Calderwood SK, (2005) Cell Stress Chaperones 10(2):86-103. (General)