|Application ||WB, IHC-P, ICC, E, IP|
|Dilution||WB (1:1000), IHC-P (1.25 µg/ml),|
|Other Names||Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27, HSPB1, HSP27, HSP28|
|Target/Specificity||Prokaryotic the full length human hsp27 protein.|
|Reconstitution & Storage||+4°C or -20°C, Avoid repeated freezing and thawing.|
|Precautions||HSPB1 / HSP27 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742).|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells Translocates to the nucleus during heat shock and resides in sub- nuclear structures known as SC35 speckles or nuclear splicing speckles.|
|Tissue Location||Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Involved in stress resistance and actin organization.
Hickey E.,et al.Nucleic Acids Res. 14:4127-4145(1986).
Carper S.W.,et al.Nucleic Acids Res. 18:6457-6457(1990).
Hino M.,et al.Biochem. Biophys. Res. Commun. 271:164-169(2000).
Briolay J.,et al.Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
Yu W.,et al.Genome Res. 7:353-358(1997).
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