HOP Protein

Human Recombinant HOP Protein

Product Specifications

Background

HOP (HSP70-HSP90 Organizing Protein) is a co-chaperone that facilitates the transfer of client proteins between HSP70 and HSP90, coordinating their folding and maturation. It acts as a scaffold, linking the two chaperone systems and ensuring efficient proteostasis under both normal and stress conditions. In the context of neurodegenerative disease, HOP is essential for managing the folding of proteins involved in neuronal signaling, cytoskeletal integrity, and synaptic function. Its role becomes particularly important in diseases characterized by protein misfolding and aggregation, such as Alzheimer’s, Parkinson’s, and ALS. HOP’s ability to regulate the chaperone cycle influences the fate of neurotoxic proteins like tau and α-synuclein. Altered HOP expression or function can disrupt this balance, leading to impaired protein clearance and neuronal dysfunction. As such, HOP is a potential therapeutic target for modulating chaperone activity and enhancing neuroprotection in degenerative brain disorders.

Product Name Alternative

HOP, HSP co chaperone, STIP1, Stress-induced-phosphoprotein 1, Hsp70/Hsp90-organizing

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

10963

Swiss Prot

P31948

Accession Number

NP_006810.1

Cellular Locus

Cytoplasm | Nucleus

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

HOP

Conjugation

His tag

Nature

Recombinant

Sequence

MGHHHHHHMEQVNELKEKGNKALSVGNIDDALQCYSEAIKLDPHNHVLYSNRSAAYAKKGDYQKAYEDGCKTVDLKPDWGKGYSRKAAALEFLNRFEEAKRTYEEGLKHEANNPQLKEGLQNMEARLAERKFMNPFNMPNLYQKLESDPRTRTLLSDPTYRELIEQLRNKPSDLGTKLQDPRIMTTLSVLLGVDLGSMDEEEEIATPPPPPPPKKETKPEPMEEDLPENKKQALKEKELGNDAYKKKDFDTALKHYDKAKELDPTNMTYITNQAAVYFEKGDYNKCRELCEKAIEVGRENREDYRQIAKAYARIGNSYFKEEKYKDAIHFYNKSLAEHRTPDVLKKCQQAEKILKEQERLAYINPDLALEEKNKGNECFQKGDYPQAMKHYTEAIKRNPKDAKLYSNRAACYTKLLEFQLALKDCEECIQLEPTFIKGYTRKAAALEAMKDYTKAMDVYQKALDLDSSCKEAADGYQRCMMAQYNRHDSPEDVKRRAMADPEVQQIMSDPAMRLILEQMQKDPQALSEHLKNPVIAQKIQKLMDVGLIAIR

Applications

WB | SDS-PAGE | Functional Assay

Field of Research

Cancer | Heat Shock

Purification Method

Affinity Purified

Purification

Affinity Purified

Limit Of Detection

This product has been certified >90% pure using SDS PAGE analysis. 4uM SPR-302, when added to 2uM SPR-300 (Aha1) -activated HSP90 (2uM; His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C, eliminated all Aha1-mediated ATPase stimulation as well as intrinsic HSP90 ATPase activity. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm) .

Concentration

Lot/batch specific. See included datasheet.

Purity

>90%

Weight

0.05

Buffer

25mM HEPES pH 7.2, 50mM NaCl, 1mM DTT, 10% glycerol

Molecular Weight

~63 kDa

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

References & Citations

1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404(1): 159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt3): 789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267: 8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9: 3638-3646.

Shipping Conditions

Blue Ice or 4ºC

Storage Conditions

-20ºC

Background Reference 01

1. Flom G., Behal R.H., Rosen L., Cole D.G., Johnson J.L. (2007) Biochem J. 404 (1) : 159-167. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt3) : 789-796. 3. Honore B.H., et al. (1992) J Biol Chem. 267: 8485-8491. 4. Nicolet C.M., et al. (1989) Mol Cell Bio. 9: 3638-3646.