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HSPE1
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. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]
Protein class
Cancer-related genes, Plasma proteins
Predicted location
Intracellular
Single cell type specificity
Cell type enhanced (Proximal tubular cells, Basal prostatic cells)
Immune cell specificity
Low immune cell specificity
Cell line specificity
Cell line enhanced (Hep G2)
Interaction
Homoheptamer arranged in a ring structure (PubMed:25918392). 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 (PubMed:25918392).
Molecular function
Chaperone
More Types Infomation
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- Derivation: Mouse
- Species Reactivity: Human
- Type: Mouse IgG1
- Application: WB, ELISA
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- Species Reactivity: Human
- Type: Mouse antibody
- Application: WB
-
- Derivation: Phage display library
- Species Reactivity: Human
- Type: Rabbit IgG
- Application: FC, IP, WB
- Rabbit Anti-HSPE1 Recombinant Antibody (clone JG82-34) (MRO-0384-CN)
-
- Species Reactivity: Human, Mouse, Rat
- Type: Rabbit IgG
- Application: WB, IHC, IP
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- Species Reactivity: Human, Mouse, Rat
- Type: Rabbit IgG
- Application: WB, IHC-P, IP
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For Research Use Only. Not For Clinical Use.