Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
HSPB11 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-144 a.a.) and having a molecular mass of 18.5kDa (Molecular weight on SDS-PAGE will appear higher).
HSPB11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Heat shock protein beta-11, Hspb11, Placental protein 25, PP25, C1orf41, HSPC034, IFT25.
MGSSHHHHHH SSGLVPRGSH MRKIDLCLSS EGSEVILATS SDEKHPPENI IDGNPETFWT TTGMFPQEFI ICFHKHVRIE RLVIQSYFVQ TLKIEKSTSK EPVDFEQWIE KDLVHTEGQL QNEEIVAHDG SATYLRFIIV SAFDHFASVH SVSAEGTVVS NLSS.
HSP90AB1 is a molecular chaperone that promotes the maturation, structural maintenance, and proper regulation of specific target proteins involved in cell cycle control and signal transduction. It undergoes a functional cycle linked to its ATPase activity, which likely induces conformational changes in client proteins, thereby causing their activation . The protein interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle, and chaperone function .
HSP90AB1 exhibits low tissue specificity and is expressed in various tissues, including the cerebral cortex, cerebellum, basal ganglia, hypothalamus, midbrain, amygdala, choroid plexus, hippocampal formation, spinal cord, retina, thyroid gland, parathyroid gland, adrenal gland, pituitary gland, lung, salivary gland, esophagus, tongue, stomach, duodenum, small intestine, colon, rectum, liver, gallbladder, pancreas, kidney, urinary bladder, testis, epididymis, seminal vesicle, prostate, vagina, ovary, fallopian tube, endometrium, cervix, placenta, breast, heart muscle, smooth muscle, skeletal muscle, adipose tissue, skin, appendix, spleen, lymph node, tonsil, bone marrow, and thymus .
HSP90AB1 is associated with various diseases, including larynx cancer and bronchitis . It is involved in critical pathways such as SARS-CoV-2 infection and inflammasomes . The protein’s role in gastric apoptosis and inflammation further underscores its importance in cellular homeostasis and disease mechanisms .
Recombinant HSP90AB1 is widely used in research to study its function and interactions with other proteins. It serves as a model to understand the mechanisms of molecular chaperones and their role in maintaining cellular integrity under stress conditions.