Anti-Hsp60 (N-terminal region) Antibody (M438)

Name: Anti-Hsp60 (N-terminal region) Antibody
Brand: PhosphoSolutions
SKU: HM4381
Price: 379.0 USD
Availability: InStock

Our Hsp60 (N-terminal region) primary antibody from PhosphoSolutions is mouse monoclonal. It detects human, mouse, and rat Hsp60 (N-terminal region) and is Protein A purified. It is great for use in WB, ICC.

Immunocytochemical labeling of Hsp60 in mitochondria in paraformaldehyde-fixed and NP40-permeabilized A7r5 cells. The cells were labeled with mouse monoclonal Hsp60 (HM4381). The antibody was detected using goat anti-mouse DyLight® 488.

Western blot image of cell structure markers in NCI-H1915 lung carcinoma cells. The blot was probed with anti-Vimentin intermediate
filament protein VM4341 (lane 1), anti-Nucleoporin p62 NM4361 (lane 2), anti-Hsp60 mitochondrial protein HM4381 (lane 3), and anti-Calnexin endoplasmic reticulum protein CM4371 (lane 4).

Immunocytochemical labeling of Hsp60 in mitochondria in paraformaldehyde-fixed and NP40-permeabilized A7r5 cells. The cells were labeled with mouse monoclonal Hsp60 (HM4381). The antibody was detected using goat anti-mouse DyLight® 488.

Click on image to zoom

Species Reactivity

Human, Mouse, Rat

Applications

ELISA, ICC, WB

Host Species

Mouse

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Data Sheet

SKU: HM4381

Volume: 100 µL

Variant

Price:

$379.00

Quantity:

Ships: 1-2 business days

Product Details

Target

Hsp60 (N-terminal region)

Scientific Background

Heat shock proteins (Hsp) are a family of highly conserved proteins that include both constitutively expressed (Hsp60, Hsp70, and Hsp90) and stress-induced (Hsp27 and Hsp72) proteins. Hsp60 is a mitochondrial protein that promotes protein folding and facilitates proteolytic degradation of misfolded or denatured proteins in the mitochondria. Hsp10 interacts with Hsp60 to regulate its substrate binding and ATPase activity. In HeLa and Jurkat mitochondria, Hsp60 associates with caspase-3 to form a complex that dissociates and releases from the mitochondria during apoptosis. Hsp60 accelerates the maturation of procaspase-3 through its ATP-dependent “foldase” activity. In addition to its protein folding activity, Hsp60 can bind the toll-like receptor-4 complex leading to production of TNFα and stimulation of a pro-inflammatory response in macrophages. Thus, the protein folding function of Hsp60 is involved in protein folding in both normal and apoptotic cells, while release of Hsp60 during necrosis is thought to stimulate a pro-inflammatory response.

Format

Protein A Purified

Clonality

Monoclonal

Clone

M438

Isotype

IgG1

Applications

ELISA, ICC, WB

Host Species

Mouse

Gene Name

HSPD1

Molecular Weight

Immunogen

Clone M438 was generated from a recombinant protein corresponding to amino acid residues in the N-terminal region of human Hsp60. This sequence has high homology to similar regions in rat and mouse Hsp60.

Immunogen Species

Human

Species Reactivity

Human, Mouse, Rat

Storage

Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Physical State

Liquid

Buffer

PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Dilution Ranges

WB: 1:1000
ICC: 1:100

Conjugate

Unconjugated

Specificity

This antibody detects a 60 kDa* protein corresponding to the apparent molecular mass of Hsp60 on SDS-PAGE immunoblots of human Jurkat and rat A7r5 cells. In immunocytochemistry, anti-Hsp60 specifically stains mitochondria in paraformaldehyde fixed and NP-40 permeabilized cells.

Quality Control

Western blots performed on each lot.

Usage Statement

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

Country of Origin

United States

Expiration

After date of receipt, stable for at least 1 year at -20°C.

Synonyms

60 kDa chaperonin; Hsp; 60 kDa heat shock protein; mitochondrial; CH60_HUMAN; Chaperonin 60; Chaperonin; 60-KD; CPN60; fa04a05; GROEL; heat shock 60kDa protein 1 (chaperonin; Heat shock protein 1 (chaperonin; Heat shock protein 60; Heat shock protein 65; heat shock protein family D (Hsp60 member 1; HLD4; Hsp 60; HSP 65; HSP-60; HSP60; HSP65; HSPD1; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; short heat shock protein 60 Hsp60s1; SPG13

UniProt ID

P10809
UniProt Summary: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).

NCBI Gene ID

3329

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Anti-Hsp60 (N-terminal region) Antibody (M438)

SKU: HM4381

Product Details

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