Anti-Hsp27 Antibody (11120)

Anti-Hsp27 Antibody (11120)

Product No.: 11120


Clone 5D12.A12 Target Hsp27 Formats AvailableView All Product Type Monoclonal Alternate Names HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27 Isotype Mouse IgG2b Applications WB,ELISA,IHC,IP


Select Product Size 100 µg — $346.00	Qty Max: Min: 1 Step: 1 $346.00 ADD TO CART Login For mAb Advantage Pricing Contact Us for Bulk Quantities


Antibody Details Product Details Reactive Species Human Host Species Mouse Immunogen Human Hsp27 Product Concentration Lot Specific Formulation PBS, pH 7.4. State of Matter Liquid Product Preparation Purified by Protein G affinity chromatography Storage and Handling This antibody is stable for at least one (1) year at -20°C. Avoid repeated freezing and thawing. Regulatory Status Research Use Only Country of Origin USA Shipping Next Day 2-8°C Applications and Recommended Usage? Quality Tested by Leinco 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 Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change. Description Description Specificity This antibody recognizes human Hsp27. 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. 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}. NCBI Gene Bank ID HSPB1 UniProt.org P04792 Research Area Heat Shock & Stress Proteins References & Citations View product citations for antibody PRODUCT_CODE on CiteAb Request COA

Antibody Details

Product Details

Reactive Species

Human

Host Species

Mouse

Immunogen

Human Hsp27

Product Concentration

Lot Specific

Formulation

PBS, pH 7.4.

State of Matter

Liquid

Product Preparation

Purified by Protein G affinity chromatography

Storage and Handling

This antibody is stable for at least one (1) year at -20°C. Avoid repeated freezing and thawing.

Regulatory Status

Research Use Only

Country of Origin

USA

Shipping

Next Day 2-8°C

Applications and Recommended Usage?
Quality Tested by Leinco

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

Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.

Description

Specificity

This antibody recognizes human Hsp27.

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.

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}.

NCBI Gene Bank ID

HSPB1

UniProt.org

P04792

Research Area

Heat Shock & Stress Proteins