JavaScript is currently not supported/disabled by this browser. Please enable JavaScript for full functionality.

Call Us 1 - 866 - 986 - 9598
orders@biohippo.com

Sign Up

Login
- My Order
- Return Requests
- Track my Order

Home / Proteins & Peptide

Human Recombinant HSP27 Protein BHP11900013

SKU : BHP11900013

Contact us to order

Tel

+1 866.986.9598

Email

orders@biohippo.com

Get a Quote

Request More Infos

StressMarq Biosciences Inc.

view supplier details

Order Now

Credit card payments now incur a 3% fee.

Contact us to order

Tel

+1 866.986.9598

Email

orders@biohippo.com

Get a Quote

Ask Merchant

Request More Infos

Sample Request

Mfr.No.	SPR-105, SPR-105A, SPR-105B, SPR-105C
Description	Human Recombinant HSP27 Protein
Alternative Names	28kDa heat shock Protein, CMT2F Protein, HSP25 Protein, HSP27 Protein, HSP28 Protein, HSPB1 Protein, SRP27 Protein
Cellular Localization	Cytoplasm, Nucleus
Certificate Of Analysis	This product has been certified >90% pure using SDS-PAGE analysis.
Field Of Use	Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.
Regulatory	RUO
Scientific Background	HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an alpha-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27 Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
Species	Human
Specificity	~27 kDa
Accession Number	BC012768
Concentration	Lot/batch specific. See included datasheet.
Purification	Affinity Purified
Expression System	E. coli
Cite This Product	Human Recombinant HSP27 Protein (StressMarq Biosciences, Canada, Cat # SPR-105C)
Mol Weight	~27 kDa
Nature	Recombinant

Gross Weight (kg)	1.4
Launch Date	09-01-2007
Net Weight (g)	0.2
Number Of Pubmed Citations	2
Swissprot	P04792
Gene Id	3315
Research Area	Cancer, Cell Signaling, Chaperone Proteins, Microfilaments, Actin, Actin Assembly, Microtubules, Tumor Biomarkers, Cardiovascular System, Atherosclerosis, Heart, Contractility, Protein Trafficking, Cytoskeleton
Target	HSP27

Adr Code	Non-hazardous
Country Of Origin	Canada
Field Of Use	Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
Published Application	Weste Blot Control ;
Published Species Reactivity	Human ;
Pubmed Id	28255900 ; 24898650
Shipping	Blue Ice or 4ºC
Stock Product	Y
Tarriff Code	3822.00.1090
Un Code For Transport	Non-hazardous
Unspsc Code	1235220
Shipping Temperature	Blue Ice or 4°C
Buffer	50mM Tris/HCl, pH8, 0.3M NaCl
Description	Accession Number: BC012768 Specificity: ~27 kDa Certificate of Analysis: This product has been certified >90% pure using SDS-PAGE analysis. Country of Origin: Canada Gross Weight (kg): 1.4 Net Weight (g): 0.05 Stock Product: Y
Purity	>90%
Storage Buffer	50mM Tris/HCl, pH8, 0.3M NaCl
Storage Temperature	-20°C

Immunogen Species	Homo Sapiens (Human)
Applications	WB, ELISA, SDS-PAGE, Functional Assay

Reference	1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell 59: 591-601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Galan A., et al. (2000) J. Biol. Chem. 275: 11418-11424. 8. Kondo T., et al. (2000) J. Biol. Chem. 275: 8872-8879. 9. Misaki T., et al. (1994) Clin. Exp. Immun. 98: 234-239. 10. Pockley A.G., et al. (1998) Immunol. Invest. 27: 367-377. 11. Moon I.S., et al. (2001) Cereb Cortex 11(3): 238-248. 12. Dressel et al. (2000) J. Immunol. 164: 2362-2371. 13. Verma A.K., et al. (2007) Fish and Shellfish Immunology. 22(5): 547-555. 14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

Product Manual	Datasheet
SDS

Have you used this product?

Rate it now..!!

Login to Review

Combination SKU	Supplier No.	Size	Your price	Quantity
BHP11900013-2	SPR-105B	100 ug	$230		Add to Cart
BHP11900013-3	SPR-105C	2X100 ug	$370		Add to Cart
BHP11900013-1	SPR-105A	50 ug	$138		Add to Cart

ebiohippo.com provides biomedical researchers with a one-stop informatic shopping experience by transforming biotechnology products’ data into a ready-to-analyze state. We collect and unify suppliers’ data on a single platform to reduce the time of searching, uncertainty, and cost of scientific experiments.

© 2025 Biohippo. All rights reserved.