HSP60 Antibody - #AF6732

(2)  
Product: HSP60 Antibody
Catalog: AF6732
Description: Rabbit polyclonal antibody to HSP60
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 60kDa; 61kD(Calculated).
Uniprot: P10809
RRID: AB_2847455

View similar products>>

   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:
Rabbit
Application:
IF/ICC 1:100-1:500, WB 1:500-1:2000
*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:
Polyclonal
Specificity:
HSP60 Antibody detects endogenous levels of total HSP60.
RRID:
AB_2847455
Cite Format: Affinity Biosciences Cat# AF6732, RRID:AB_2847455.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , 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.

Uniprot:

P10809(CH60_HUMAN) >>Visit HPA database.

Gene(ID):
HSPD1(3329)
Sequence:
MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

PTMs - P10809 As Substrate

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

Research Backgrounds

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.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.