Rabbit Polyclonal HSPA4 antibody. Suitable for WB and reacts with Trypanosoma brucei samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Trypanosoma brucei brucei Heat shock 70 kDa protein 4 aa 200-300.
View Alternative Names
Heat shock 70 kDa protein 4, HSP70-4
- WB
Supplier Data
Western blot - Anti-Hsp70 antibody (AB240902)
Primary incubation for 2 hours at room temperature.
Block : 5% Skim Milk in 1X TBST.
All lanes:
Western blot - Anti-Hsp70 antibody (ab240902) at 1/1000 dilution
Lane 1:
Trypanosoma brucei brucei (cells incubated at 37°C) cell lysate at 15 µg
Lane 2:
Trypanosoma brucei brucei (cells incubated for 1 hour at 42°C) cell lysate at 15 µg
Secondary
All lanes:
Goat Anti-Rabbit IgG: HRP at 1/3000 dilution
Predicted band size: 70 kDa
true
Exposure time: 5min
Reactivity data
Properties and storage information
Form
Purification technique
Storage buffer
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Hsp70 operates by stabilizing intermediate states of folding proteins preventing aggregation and facilitating the correct folding process. It often forms a complex with co-chaperones such as Hsp40 and nucleotide exchange factors. This complex is essential for the protein's activity and function. Additionally Hsp70 participates in protein degradation pathways by guiding misfolded proteins to the proteasome for degradation maintaining cellular homeostasis.
Pathways
This molecular chaperone plays significant roles in the heat shock response and unfolded protein response pathways. Hsp70 interacts closely with proteins such as Hsp90 and co-chaperones which together help protect cells from stress-induced damage. The protein also participates in the JAK/STAT signaling pathway influencing cell proliferation and apoptosis. These interactions suggest an integral role in maintaining cellular integrity during stress conditions.
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Publications (1)
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EXCLI journal 19:1141-1153 PubMed33013268
2020
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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