Product: HSP10 Antibody
Catalog: AF0183
Description: Rabbit polyclonal antibody to HSP10
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Rabbit, Chicken, Xenopus
Mol.Wt.: 10kDa; 11kD(Calculated).
Uniprot: P61604
RRID: AB_2833376

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

Product Info

Source:
Rabbit
Application:
WB 1:500-1:3000, IHC 1:50-1:200, 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
Prediction:
Pig(100%), Zebrafish(83%), Bovine(100%), Horse(100%), Rabbit(100%), Chicken(83%), Xenopus(94%)
Clonality:
Polyclonal
Specificity:
HSP10 Antibody detects endogenous levels of total HSP10.
RRID:
AB_2833376
Cite Format: Affinity Biosciences Cat# AF0183, RRID:AB_2833376.
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

10 kDa chaperonin; 10 kDa heat shock protein mitochondrial; 10 kDa heat shock protein, mitochondrial; CH10_HUMAN; Chaperonin 10; Chaperonin 10 homolog; CPN10; cpn10 homolog; Early pregnancy factor; Early-pregnancy factor; EPF; GROES; GroES homolog; Heat shock 10kD protein 1 chaperonin 10; Heat shock 10kDa protein 1; Heat shock 10kDa protein 1 chaperonin 10; Heat-shock 10-kD protein; Hsp10; Hspe1;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
HSPE1 Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. Belongs to the groES chaperonin family. Induced by stress. Homohexamer.
Sequence:
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGSKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Rabbit
100
Xenopus
94
Zebrafish
83
Chicken
83
Sheep
0
Dog
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P61604 As Substrate

Site PTM Type Enzyme
M1 Acetylation
K8 Acetylation
K8 Methylation
K8 Ubiquitination
R15 Methylation
S21 Phosphorylation
T27 Phosphorylation
K28 Ubiquitination
K36 Methylation
K36 Ubiquitination
S37 Phosphorylation
K40 Acetylation
K40 Ubiquitination
T45 Phosphorylation
S51 Phosphorylation
S53 Phosphorylation
K56 Acetylation
K56 Ubiquitination
S64 Phosphorylation
K66 Ubiquitination
K70 Acetylation
K70 Ubiquitination
Y76 Phosphorylation
T79 Phosphorylation
K80 Acetylation
K80 Sumoylation
K80 Ubiquitination
K86 Acetylation
K86 Ubiquitination
Y88 Phosphorylation
R92 Methylation
K99 Acetylation
K99 Ubiquitination

Research Backgrounds

Function:

Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, 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. 2 heptameric Hsp10 rings interact with a Hsp60 tetradecamer in the structure of a back-to-back double heptameric ring to form the symmetrical football complex.

Family&Domains:

Belongs to the GroES chaperonin family.

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.