Abcam, ab154409, Anti-HSPA1L antibody

Size: 100µL
Rabbit Polyclonal HSPA1L antibody. Suitable for IHC-P, WB, ICC/IF and reacts with Human, Rat, Mouse samples. Cited in 6 publications. Immunogen corresponding to Recombinant Fragment Protein within Human Heat shock 70 kDa protein 1-like aa 1-300.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:ICC/IF, WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human Heat shock 70 kDa protein 1-like aa 1-300. The exact immunogen used to generate this antibody is proprietary information.P34931

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Storage buffer-pH: 7Preservative: 0.01% Thimerosal (merthiolate)Constituents: 10% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HSPA1L also known as heat shock 70 kDa protein 1-like is a member of the heat shock protein 70 family. It functions as a molecular chaperone assisting in proper protein folding and preventing aggregation of misfolded proteins. The protein has a molecular mass of approximately 70 kDa. HSPA1L expression is observed in various human tissues with notable presence in testis and brain indicating roles in these organs.
Biological function summary
Heat shock proteins including HSPA1L play significant roles in stress response and cellular homeostasis. HSPA1L does not usually function alone; it often forms part of complexes with other molecular chaperones and co-chaperones to effectively carry out its roles. By stabilizing new proteins and repairing damaged ones it contributes to cell survival under stress conditions such as heat shock and oxidative stress.
Pathways
Several signaling pathways involve the action of HSPA1L. It actively participates in the protein quality control system and is a component of the cellular response to stress stimuli. Key pathways include the protein refolding and apoptosis pathways. HSPA1L interacts with other heat shock proteins like HSP70 and co-chaperones such as HSP40 to perform refolding tasks and to regulate apoptotic signals maintaining cellular stability under various conditions.
HSPA1L has associations with several pathologies reflecting its stress response functions. Research links it to neurodegenerative diseases like Alzheimer's where protein aggregation is a feature. HSPA1L is also connected to cancer where its chaperoning activity could interact with oncogenes and tumor suppressor proteins. These associations emphasize the importance of HSPA1L in maintaining proteostasis and implicate it in the pathological processes when proteostasis is disrupted.