Recombinant Human Hsp40 Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >=80% purity, <= 0.03 EU/µg endotoxin level and suitable for SDS-PAGE, sELISA.
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Key facts
- Purity
>=80% SDS-PAGE
- Endotoxin level
<= 0.03 EU/µg
- Expression system
Escherichia coli
- Tags
His tag C-Terminus
- Applications
SDS-PAGE, sELISA
- Biologically active
No
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application sELISA | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877).
Alternative names
DnaJ homolog subfamily B member 1, DnaJ protein homolog 1, Heat shock 40 kDa protein 1, Human DnaJ protein 1, HSP40, Heat shock protein 40, hDj-1, HSPF1, HDJ1, DNAJ1, DNAJB1
Recommended products
Recombinant Human Hsp40 Protein Standard (His tag) is a Human Fragment protein, expressed in Escherichia coli, with >=80% purity, <= 0.03 EU/µg endotoxin level and suitable for SDS-PAGE, sELISA.
Alternative names
DnaJ homolog subfamily B member 1, DnaJ protein homolog 1, Heat shock 40 kDa protein 1, Human DnaJ protein 1, HSP40, Heat shock protein 40, hDj-1, HSPF1, HDJ1, DNAJ1, DNAJB1
Key facts
- Purity
>=80% SDS-PAGE
- Endotoxin level
<= 0.03 EU/µg
- Expression system
Escherichia coli
- Tags
His tag C-Terminus
- Applications
SDS-PAGE, sELISA
- Biologically active
No
- Accession
- P25685-1
- Animal free
Yes
- Species
Human
- Concentration
- Storage buffer
pH: 7.3 - 7.5
Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic
Sequence info
Amino acid sequence
- Accession
- Protein length
Fragment
- Predicted molecular weight
39.9 kDa
- Nature
Recombinant
- Tags
His tag C-Terminus
Specifications
- Form
Liquid
General info
- Function
Interacts with HSP70 and can stimulate its ATPase activity. Stimulates the association between HSC70 and HIP. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) (PubMed:24318877).
- Subcellular localisation
Nucleus, Nucleolus
Storage
- Shipped at conditions
Dry Ice
- Appropriate short-term storage conditions
-80°C
- Appropriate long-term storage conditions
-80°C
- Aliquoting information
Upon delivery aliquot
- Storage information
Avoid freeze / thaw cycle
Supplementary info
- Activity summary
Hsp40 also known as DnaJB1 is a member of the heat shock protein family that acts mechanically as a molecular chaperone. This protein with a mass of approximately 41 kDa assists in protein folding and stabilization preventing aggregation under stress conditions. Hsp40 proteins are widely expressed in various tissues and are important in maintaining cellular homeostasis. In addition to DnaJB1 other aliases include 3b9 and 2a7 which emphasize its variety within the Hsp40 family.
- Biological function summary
Hsp40 proteins participate in cell signaling and stress response by modulating the activity of Hsp70 forming a functional complex with it to guide protein folding processes. This process is essential for protein quality control and cellular protection. It interacts with unfolded proteins and delivers them to Hsp70 enhancing its ATPase activity necessary for the proper functioning of these molecular chaperones. The expression of Hsp40 in stress conditions highlights its importance in the protein quality control system.
- Pathways
Hsp40 is involved in important cellular mechanisms like the unfolded protein response and protein catabolism pathways. It works closely with Hsp70 playing a pivotal role in managing protein misfolding and aggregation vital for cellular stress response and recovery. In these pathways Hsp40's function ensures the proper folding and degradation of damaged proteins maintaining proteostasis in the cell.
- Associated diseases and disorders
Hsp40 influences the development of neurodegenerative diseases and certain cancers. Mutations or altered expression of Hsp40 can lead to disrupted protein homeostasis contributing to conditions like Alzheimer's disease and tumor progression. In Alzheimer's disease besides interacting with Hsp70 Hsp40 affects the accumulation of amyloid-beta peptides. In cancer contexts it may interact with other chaperone proteins affecting their function and therefore promoting tumor aggressiveness and resistance to stress.
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2 product images
SDS-PAGE - Recombinant Human Hsp40 Protein Standard (His tag) (ab316297)
SDS-PAGE analysis of ab316297.
Sandwich ELISA - Recombinant Human Hsp40 Protein Standard (His tag) (ab316297)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
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Product protocols
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