HSP60 Mouse Monoclonal Antibody | Affinity Biosciences

WB
IF/ICC

1/2

Western blot analysis of extracts from various samples, using HSP60 Mouse Monoclonal Antibody.

Product:	HSP60 Mouse Monoclonal Antibody
Catalog:	BF8045
Description:	Mouse monoclonal antibody to HSP60
Application:	WB IF/ICC
Reactivity:	Human, Mouse, Rat
Prediction:	Zebrafish, Bovine, Horse, Sheep, Rabbit, Xenopus
Mol.Wt.:	60 kDa; 61kD(Calculated).
Uniprot:	P10809

View similar products>>

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

Size	Price	Inventory
100ul	$280	In stock
200ul	$350	In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Related Downloads

MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Mouse

Application:

WB 1:500-1:3000, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:

Human,Mouse,Rat

Clonality:

Monoclonal [AFfirm8045(AFP21842)]

Specificity:

HSP60 Antibody detects endogenous levels of total HSP60.

Conjugate:

Unconjugated.

Purification:

Affinity-chromatography.

Storage:

Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

Alias:

Fold/Unfold

60 kDa chaperonin; 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;

Immunogens

Immunogen:

A synthesized peptide derived from human HSP60, corresponding to a region within C-terminal amino acids.

Uniprot:

P10809(CH60_HUMAN) >>Visit HPA database.

Gene(ID):

HSPD1(3329)

Description:

Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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.

Sequence:

P10809 CH60_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

PTMs - P10809 As Substrate

P10809

Site	PTM Type	Source
R3	Methylation	Uniprot
K31	Acetylation	Uniprot
K31	Ubiquitination	Uniprot
K58	Ubiquitination	Uniprot
T61	Phosphorylation	Uniprot
S67	Phosphorylation	Uniprot
S70	Phosphorylation	Uniprot
K72	Ubiquitination	Uniprot
T74	Phosphorylation	Uniprot
K75	Ubiquitination	Uniprot
T79	Phosphorylation	Uniprot
K82	Acetylation	Uniprot
K82	Ubiquitination	Uniprot
S83	Phosphorylation	Uniprot
K87	Acetylation	Uniprot
K87	Ubiquitination	Uniprot
Y90	Phosphorylation	Uniprot
K91	Acetylation	Uniprot
K91	Ubiquitination	Uniprot
K96	Acetylation	Uniprot
K96	Ubiquitination	Uniprot
T105	Phosphorylation	Uniprot
T113	Phosphorylation	Uniprot
T114	Phosphorylation	Uniprot
T115	Phosphorylation	Uniprot
K125	Acetylation	Uniprot
K125	Ubiquitination	Uniprot
K130	Acetylation	Uniprot
K130	Ubiquitination	Uniprot
S132	Phosphorylation	Uniprot
K133	Acetylation	Uniprot
K133	Ubiquitination	Uniprot
R141	Methylation	Uniprot
K156	Acetylation	Uniprot
K157	Acetylation	Uniprot
S159	Phosphorylation	Uniprot
K160	Ubiquitination	Uniprot
T164	Phosphorylation	Uniprot
K180	Acetylation	Uniprot
S187	Phosphorylation	Uniprot
K191	Acetylation	Uniprot
K191	Ubiquitination	Uniprot
K192	Acetylation	Uniprot
K196	Ubiquitination	Uniprot
T200	Phosphorylation	Uniprot
K202	Acetylation	Uniprot
K202	Ubiquitination	Uniprot
T206	Phosphorylation	Uniprot
K218	Acetylation	Uniprot
K218	Ubiquitination	Uniprot
R221	Methylation	Uniprot
Y223	Phosphorylation	Uniprot
S225	Phosphorylation	Uniprot
Y227	Phosphorylation	Uniprot
T231	Phosphorylation	Uniprot
S232	Phosphorylation	Uniprot
K233	Acetylation	Uniprot
K233	Ubiquitination	Uniprot
K236	Acetylation	Uniprot
K236	Ubiquitination	Uniprot
C237	S-Nitrosylation	Uniprot
Y243	Phosphorylation	Uniprot
S247	Phosphorylation	Uniprot
K249	Acetylation	Uniprot
K249	Ubiquitination	Uniprot
K250	Ubiquitination	Uniprot
S252	Phosphorylation	Uniprot
S253	Phosphorylation	Uniprot
S256	Phosphorylation	Uniprot
K269	Acetylation	Uniprot
K292	Methylation	Uniprot
K292	Ubiquitination	Uniprot
K301	Ubiquitination	Uniprot
K352	Acetylation	Uniprot
K352	Ubiquitination	Uniprot
K359	Acetylation	Uniprot
K359	Ubiquitination	Uniprot
K364	Acetylation	Uniprot
K369	Acetylation	Uniprot
K369	Ubiquitination	Uniprot
T381	Phosphorylation	Uniprot
T382	Phosphorylation	Uniprot
S383	Phosphorylation	Uniprot
Y385	Phosphorylation	Uniprot
K387	Acetylation	Uniprot
K389	Acetylation	Uniprot
K396	Acetylation	Uniprot
K396	Ubiquitination	Uniprot
S398	Phosphorylation	Uniprot
T409	Phosphorylation	Uniprot
S410	Phosphorylation	Uniprot
K417	Acetylation	Uniprot
K417	Ubiquitination	Uniprot
T422	Phosphorylation	Uniprot
T428	Phosphorylation	Uniprot
C442	S-Nitrosylation	Uniprot
C447	S-Nitrosylation	Uniprot
T455	Phosphorylation	Uniprot
K462	Acetylation	Uniprot
K469	Acetylation	Uniprot
K469	Ubiquitination	Uniprot
T471	Phosphorylation	Uniprot
K473	Acetylation	Uniprot
K473	Ubiquitination	Uniprot
T478	Phosphorylation	Uniprot
K481	Ubiquitination	Uniprot
S488	Phosphorylation	Uniprot
S498	Phosphorylation	Uniprot
S499	Phosphorylation	Uniprot
Y503	Phosphorylation	Uniprot
K516	Acetylation	Uniprot
K516	Methylation	Uniprot
K516	Ubiquitination	Uniprot
T522	Phosphorylation	Uniprot
K523	Acetylation	Uniprot
K523	Ubiquitination	Uniprot
T527	Phosphorylation	Uniprot
T540	Phosphorylation	Uniprot
K551	Acetylation	Uniprot

Research Backgrounds

P10809_CH60_HUMAN

Function:

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).

Subcellular Location:

Mitochondrion matrix.

Subunit Structure:

Homoheptamer arranged in a ring structure. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex. Interacts with HRAS (By similarity). Interacts with ATAD3A. Interacts with ETFBKMT and METTL21B. Interacts with MFHAS1.

(Microbial infection) Interacts with hepatits B virus/HBV protein X.

(Microbial infection) Interacts with HTLV-1 protein p40tax.

Family&Domains:

Belongs to the chaperonin (HSP60) family.

Research Fields

· Genetic Information Processing > Folding, sorting and degradation > RNA degradation.

· Human Diseases > Endocrine and metabolic diseases > Type I diabetes mellitus.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

Restrictive clause

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.

HSP60 Mouse Monoclonal Antibody - #BF8045