Rabbit Polyclonal STCH antibody. Suitable for WB, ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human HSPA13 aa 200-400.
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 78.99% PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Polyclonal
WB | ICC/IF | |
---|---|---|
Human | Tested | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/500.00000 - 1/3000.00000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/100.00000 - 1/1000.00000 | Notes - |
Select an associated product type
Heat shock 70 kDa protein 13, Microsomal stress-70 protein ATPase core, Stress-70 protein chaperone microsome-associated 60 kDa protein, STCH, HSPA13
Rabbit Polyclonal STCH antibody. Suitable for WB, ICC/IF and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human HSPA13 aa 200-400.
Heat shock 70 kDa protein 13, Microsomal stress-70 protein ATPase core, Stress-70 protein chaperone microsome-associated 60 kDa protein, STCH, HSPA13
IgG
Rabbit
pH: 7
Preservative: 0.01% Thimerosal (merthiolate)
Constituents: 78.99% PBS, 20% Glycerol (glycerin, glycerine), 1% BSA
Liquid
Polyclonal
Affinity purification Immunogen
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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This supplementary information is collated from multiple sources and compiled automatically.
STCH also known as Stress-70 protein chaperone is an important molecular chaperone belonging to the Hsp70 family. It weighs approximately 66 kDa and is mainly expressed in the endoplasmic reticulum. STCH helps in protein folding and preventing aggregation which is necessary for maintaining protein homeostasis. This protein's function is less understood compared to other Hsp70 homologs but is believed to be activated under stress conditions like heat shock.
STCH participates in managing protein maturation and degradation processes. It works by stabilizing nascent polypeptide chains and assisting in their proper folding though not always forming stable complexes with other proteins. Its localization to the endoplasmic reticulum suggests a specific role in dealing with secretory and membrane proteins. This chaperone guards the cellular proteostasis against stress-induced misfolding a critical process in maintaining normal cellular function.
STCH is involved in the unfolded protein response (UPR) and other stress-related pathways. The UPR plays a role in cellular stress management and signaling mechanisms. STCH interacts with other chaperones like BiP/GRP78 and GRP94 which are significant in these pathways. Through its activity STCH contributes to protein quality control and mitigates proteotoxic stress which affects cellular health and function.
The role of STCH appears in neurodegenerative diseases and cancer. Misregulation of chaperone proteins like STCH can contribute to the progression of Alzheimer's disease through its impact on proteostasis and amyloid-beta peptide folding. In cancer association with proteins such as Hsp90 indicates STCH's influence on tumor growth and survival possibly offering a target for therapeutic intervention. Understanding STCH's function in these contexts remains an active research area.
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All lanes: Western blot - Anti-STCH antibody (ab127750) at 1/500 dilution
All lanes: U-87 MG whole cell lysate at 30 µg
Performed under reducing conditions.
Predicted band size: 51 kDa
ab127750 at 1/500 dilution staining STCH in methanol-fixed Hela cells by Immunofluorescence.
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