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Mouse Anti-HSPE1 Recombinant Antibody (4C11-B11) (CBMAB-A4147-LY)

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Basic Information

Host Animal
Mouse
Clone
4C11-B11
Application
WB, ELISA
Immunogen
HSPE1 (AAH23518, 1 a.a. ~ 102 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
More Infomation

Target

Full Name
heat shock 10kDa protein 1 (chaperonin 10)
Introduction
This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. [provided by RefSeq]
Entrez Gene ID
3336
UniProt ID
P61604
Alternative Names
CPN10; GROES; HSP10
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 (PubMed:7912672, PubMed:1346131, PubMed:11422376).

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).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Chaperone cofactor-dependent protein refolding Source: GO_Central
Osteoblast differentiation Source: UniProtKB
Protein folding Source: ProtInc
Response to unfolded protein Source: ProtInc
Cellular Location
Mitochondrion matrix

Yeung, N., Murata, D., Iijima, M., & Sesaki, H. (2023). Role of human HSPE1 for OPA1 processing independent of HSPD1. Iscience, 26(2).

Boudreault, J., Wang, N., Yan, G., Dai, M., Poulet, S., Daliah, G., & Lebrun, J. J. (2023). In vivo genome-wide CRISPR screen in pancreatic ductal adenocarcinoma defines HSPE1 as a potential oncogene by acting through G2/M cell cycle arrest. Cancer Research, 83(7_Supplement), 3938-3938.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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