Anti-Hsp27 Antibody

Mouse Monoclonal Antibody specific to Hsp27

Product Specifications

CAS Number

9007-83-4

Product Name Alternative

HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27

Gene Name

HSPB1

Gene ID

3315

NCBI Gene ID

UniProt

P04792

Accession Number

NP_001531.1

Cellular Locus

Cytoplasm, Nucleus, Cytoplasm, cytoskeleton, spindle

Host

Mouse

Reactivity

Human

Immunogen

Human Hsp27

Target Antigen

Heat shock protein beta-1

Target

Hsp27

Clonality

Monoclonal

Isotype

IgG2b

Type

Antibody

Applications

WB, ELISA, IHC, IP

Field of Research

Heat Shock& Stress Proteins

Purification Method

Purified by Protein G affinity chromatography

Concentration

Lot Specific

Dilution

Dilute in PBS or medium which is identical to that used in the assay system.

Format

Purified

Form

Liquid

Buffer

Phosphate Buffered Saline

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). {PubMed:10383393, PubMed:19166925, PubMed:20178975, PubMed:23728742}.

Additionnal Information

Immunoblotting: use at 0.5-1ug/ml. A band of 27 kDa is detected ELISA: use at 1ug/ml. Immunohistochemistry: use at 1- 10ug/ml. Immunoprecipitation: use at 1-10ug/ml. Positive control: HeLa cell lysate

Storage Conditions

This antibody is stable for at least one (1) year at -20°C.

Specificity

This antibody recognizes human Hsp27.

Formulation

PBS, pH 7.4.

Buffer pH

pH 7.4

Target Background

Hsp27 is an important heat shock protein found in normal and malignant human cells. The basic structure of most Hsps is a highly conserved amino acid sequence with an alpha-crystallin domain at the C-terminus and WD/EPF domain at the less conserved N- terminus. The N-terminus is essential for formation of high molecular weight oligomers. Hsp27 oligomers are formed by as many as 8-40 Hsp 27 monomers. The degree of oligomerization is associated with chaperone activity: large oligomers have high chaperone activity, whereas dimers have no chaperone activity. Hsp27 is localized in 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. Hsp27 is also involved in the apoptotic signaling pathway because it interferes with activation of cytochrome C / Apaf-1 / dATP complex, thereby inhibiting activation of procaspase-9.