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LearnADI-SPA-803-F
antibody from Enzo Life Sciences
Targeting: HSPB1
CMT2F, Hs.76067, Hsp25, HSP27, HSP28
Western blot
ELISA
ImmunocytochemistryAntibody data
- Antibody Data
- Antigen structure
- References [8]
- Comments [0]
- Validations
- Immunocytochemistry [2]
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- Product number
- ADI-SPA-803-F - Provider product page
- Provider
- Enzo Life Sciences
- Product name
- HSP27 polyclonal antibody
- Antibody type
- Polyclonal
- Antigen
- Recombinant full length protein
- Description
- Protein A affinity purified.
- Reactivity
- Human, Porcine, Simian
- Host
- Rabbit
- Vial size
- 200 μg
- Storage
- -20°C
- Handling
- Avoid freeze/thaw cycles.
Submitted references Heat shock protein 27 promotes cell proliferation through activator protein-1 in lung cancer.
Acute response and subcellular movement of HSP27, αB-crystallin and HSP70 in human skeletal muscle after blood-flow-restricted low-load resistance exercise.
Methylglyoxal alters the function and stability of critical components of the protein quality control.
The small heat shock protein 27 is a key regulator of CD8+ CD57+ lymphocyte survival.
Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay.
Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans.
Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27.
Overexpression of the human 72 kDa heat shock protein in renal tubular cells confers resistance against oxidative injury and cisplatin toxicity.
Zhang S, Hu Y, Huang Y, Xu H, Wu G, Dai H
Oncology letters 2015 Jun;9(6):2572-2576
Oncology letters 2015 Jun;9(6):2572-2576
Acute response and subcellular movement of HSP27, αB-crystallin and HSP70 in human skeletal muscle after blood-flow-restricted low-load resistance exercise.
Cumming KT, Paulsen G, Wernbom M, Ugelstad I, Raastad T
Acta physiologica (Oxford, England) 2014 Aug;211(4):634-46
Acta physiologica (Oxford, England) 2014 Aug;211(4):634-46
Methylglyoxal alters the function and stability of critical components of the protein quality control.
Bento CF, Marques F, Fernandes R, Pereira P
PloS one 2010 Sep 24;5(9):e13007
PloS one 2010 Sep 24;5(9):e13007
The small heat shock protein 27 is a key regulator of CD8+ CD57+ lymphocyte survival.
Wood KL, Voss OH, Huang Q, Parihar A, Mehta N, Batra S, Doseff AI
Journal of immunology (Baltimore, Md. : 1950) 2010 May 15;184(10):5582-8
Journal of immunology (Baltimore, Md. : 1950) 2010 May 15;184(10):5582-8
Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay.
Sinsimer KS, Gratacós FM, Knapinska AM, Lu J, Krause CD, Wierzbowski AV, Maher LR, Scrudato S, Rivera YM, Gupta S, Turrin DK, De La Cruz MP, Pestka S, Brewer G
Molecular and cellular biology 2008 Sep;28(17):5223-37
Molecular and cellular biology 2008 Sep;28(17):5223-37
Maximal eccentric exercise induces a rapid accumulation of small heat shock proteins on myofibrils and a delayed HSP70 response in humans.
Paulsen G, Vissing K, Kalhovde JM, Ugelstad I, Bayer ML, Kadi F, Schjerling P, Hallén J, Raastad T
American journal of physiology. Regulatory, integrative and comparative physiology 2007 Aug;293(2):R844-53
American journal of physiology. Regulatory, integrative and comparative physiology 2007 Aug;293(2):R844-53
Cell death inhibiting RNA (CDIR) derived from a 3'-untranslated region binds AUF1 and heat shock protein 27.
Shchors K, Yehiely F, Kular RK, Kotlo KU, Brewer G, Deiss LP
The Journal of biological chemistry 2002 Dec 6;277(49):47061-72
The Journal of biological chemistry 2002 Dec 6;277(49):47061-72
Overexpression of the human 72 kDa heat shock protein in renal tubular cells confers resistance against oxidative injury and cisplatin toxicity.
Komatsuda A, Wakui H, Oyama Y, Imai H, Miura AB, Itoh H, Tashima Y
Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 1999 Jun;14(6):1385-90
Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 1999 Jun;14(6):1385-90
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Supportive validation
- Submitted by
- Enzo Life Sciences (provider)
- Main image
- Experimental details
- Western blot analysis of HSP27 pAb: Lane 1: MW marker, Lane 2: HSP27 Recombinant Human Protein, Lane 3: HSP25 Recombinant Murine Protein (Negative Control), Lane 4: HeLa, Lane 5: HeLa, Heat Shocked, Lane 6: Vero, Heat Shocked, Lane 7: 3T3, Heat Shocked, Lane 8: PC-12, Heat Shocked.
- Submitted by
- Enzo Life Sciences (provider)
- Main image
- Experimental details
- Immunohistochemistry analysis of human heart tissue stained with HSP27, pAb at 10µg/ml.
