HSP90AB1 Antibodies

Heat shock protein HSP 90-beta (HSP90AB1)

Molecular chaperone that promotes the maturation, structural maintenance and appropriate regulation of specific target proteins involved for example in cell cycle control and signal transduction. Undergoes a functional cycle that is connected to its ATPase activity.

This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that govern its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785).

Gene Information

Human
Gene Name:	HSP90AB1
Uniprot:	P08238
Entrez:	3326

Family

Belongs to:
heat shock protein 90 family

Alternative Names

D6S182; Heat shock 84 kDa; heat shock 90kD protein 1, beta; heat shock 90kDa protein 1, beta; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein beta; heat shock protein HSP 90-beta; HSP 84; HSP84; HSP90 beta; HSP90AB1; HSP90B; HSP90-BETA; HSP90BHSP 90; HSPC2; HSPC2D6S182; HSPCB; HSPCBFLJ26984

Molecular Weight

Mass (kDA):
83.264 kDA

Genomic Context

Human
Location:	6p21.1
Sequence:	6; NC_000006.12 (44246166..44253888)

Subcellular Localizations

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762).

Diseases

• Malignant Neoplasms
• Neoplasms
• Carcinoma
• Infertility
• Ovarian Neoplasm
• Liver Carcinoma
• Inflammation
• Hepatitis B
• Hepatitis
• Osteoarthritis, Knee
• Malignant Neoplasm Of Ovary
• Neuroblastoma
• Sclerosis

• Malignant Neoplasm Of Breast
• Mammary Neoplasms
• Liver Neoplasms
• Cell Transformation, Neoplastic
• Multiple Sclerosis
• Leukemia
• Autoimmunity

Pathways

• Cell Proliferation
• Cell Growth
• Pathogenesis
• Translation
• Secretion
• Flight
• Cell Cycle
• Chromatin Remodeling
• Response To Stress
• Localization
• Cytokine Production
• Protein Folding
• Rna Interference

• Transport
• Protein Phosphorylation
• Hibernation
• Cell Migration
• Gene Silencing
• Cellular Homeostasis
• Protein Maturation

PTMs

• Phosphorylation
• Biotinylation
• Cleavage
• Nitrosylation

• Glycosylation
• Acetylation
• Methylation
• Dephosphorylation

• Ubiquitination

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/HSP90AB1

Best Uses Of The HSP90AB1 Marker

The Heat Shock Protein HSP90AB1 a chaperone protein encoded by the gene. It is used to distinguish cancer patients from non-cancer patients. This article will explore its benefits and potential uses. Let's begin by defining what this protein is and how it's detected. Find out more here. Here are the Best Uses Of The HSP90AB1 Marker

Heat shock protein HSP 90-beta is a protein that in humans is encoded by the HSP90AB1 gene.

The HSP90AB1 human gene encodes HSP 90-beta. This protein is an essential component of the cellular immune system. The protein is comprised of four domains: ER, endoplasmic reticulum (ER), mitochondria, and nuclear membrane. The protein is extremely conserved and can be classified into four classes in accordance with its sequence conservation. HSP90 proteins can be separated into two groups, each having distinct amino acid sequences.

The human genome database includes 894 genes encoding HSP90-beta. Six of them were confirmed by mRNA sequences, and two were new predictions based on NCBI annotation. The remaining eight were not supported. The gene code for HSP90AB1 is located on the 4q23 chromosome.

Two copies of HSP90AB1 can be found in the human genome: HSP90AA1-1 and HSP90AB1-1. The two genes are paralogous. Both proteins are highly conserved and have the same gene sequence. Both human proteins share a common ancestor, however, there are distinct differences between them. HSP90AB is more closely related to HSP90AA.

In humans in humans, the HSP90AB1 gene encodes the heat shock protein HSP90-beta. HSP90AB1 encodes an identical protein to HSP90AA1. Although the HSP90AB1 gene encodes a different protein, they are located on one chromosome.

Humans have two copies of the gene, HSP90AB1. Both versions of the protein are highly conserved molecular chaperones. They play crucial roles in signal transduction as well as protein folding. They are involved in the degradation process of proteins that have been denatured as well being able to stabilize them. HSP90AB1 also interacts with co-chaperones, including UNC45A CHORDC1, DNAJC7, FKBP4 and HSP90AB1.

It is crucial to keep in mind that different types and levels of heat-shock proteins can be expressed at different levels of expression and their sensitivity when comparing proteins. The heat shock proteins can impact the way the immune system functions. The genes that control the function of the HSP90AB1 gene are expressed and function in a variety of cells. These variants aren't necessarily connected to any particular illness or disease.

Variants can also be used to characterize the gene. The HSP90AB1 gene encodes heat shock protein. The HSP90AB1 variants differ with respect to codons they use. The first variant uses an inserting a splice site in the 5' UTR, and the second variant employs an in-frame splicing location in the internal code region.

It is a chaperone protein.

The heat shock protein 90 kDa class B member 1 (HSP90AB1) is a molecular chaperone with a high degree of conservation. It is highly expressed in different cancer cells that include non-small-cell lung cancer. HSP90AB1 is involved in numerous pathophysiological processes by interacting with the client proteins. This study investigates the significance of clinical studies and the expression of HSP90AB1 in cancer cells.

The role of HSP90AB1 the growth of cancerous cells is unclear. It could influence the expression of Bcr Abl in cells by interfering with its transfer to the nucleus. Although the effects of HSP90AB1 inhibitors on cell growth aren't clear, these data are promising for the development and use of an HSP90 inhibitor for the treatment of Bcr-Abl-addicted malignancies.

This study involved two separate cohorts of GC patients. The first cohort comprised 150 patients suffering from primary GC who underwent radical surgery at Nanfang Hospital between 2013 and between 2013 and. The participants provided written informed consent, and were evaluated using real-time PCR in a quantitative manner. Western Blotting and Immunohistochemistry were used to validate the expression of HSP90AB1.

HSP90AB1 inhibits ubiquitin-mediated degradation of LRP5 which is an anti-tumor agent. This protein is also essential in the endoplasmic Reticulum's (ER) folding of proteins. Its expression is highly increased in solid tumors, where it is thought to promote the epithelial-mesenchymal transition. In contrast to its intracellular counterpart, HSP90AB1 hinders the growth of gastric cancer cells and also inhibits the growth of solid tumors.

The interaction between estrogen and ESRI has been observed to alter the expression of HSP90 proteins in avian tissues. The HSP90 protein also facilitates the interaction of ESRI with OCs. HSP90AB1 blocks ESR1's hormone binding conformation in avian tissues. This makes calcium not accessible for eggshell formation, creating a thin shell syndrome.

We used lentiviral vectors that expressed HSP90AB1 as well as a control vector for cultivate cells to conduct the experiments. After transfection, cells were incubated for 30 mM the MG132. The cells were then lysed with RIPA buffer, which contains an inhibitor of proteinase. To confirm the presence of immunoprecipitated proteins western blot and DNA sequencing were carried out.

In addition to being a transcription factor, HSP90AB1 also promotes cell expansion and migration by stimulating the production of CCK-8 and phosphorylated AKT. HSP90AB1 is also known to block the activity of bcatenin and the Wnt/bcatenin pathway of signaling. HSP90AB1 is also a major player in regulating cell proliferation, migration, and invasion in GC cells.

HSP90AB1 overexpression in human gastric cancer cells increased cell migration, invasion, and growth. Hsp90AB1 expression in human gastric cancer cells increased the sensitivity to chemotherapy as well as the growth of tumors in a mouse model of xenograft. These findings suggest that Hsp90AB1 could promote metastasis. This is the first study to show HSP90AB1's involvement in GC.

It may be used to differentiate cancer from noncancer patients

Boster Bio has identified a new biomarker for the detection of breast cancers that have up-regulated Hsp90 proteins. This gene is also known as HSP90AB1. It is expressed at a much higher level in breast cancer tissues than in healthy tissues. It could be used in the near future to differentiate cancer patients from non-cancer ones, although there is still a lot to learn.

Although this study is still in its preliminary stage however, it suggests that Boster Bio’s HSP90AB1 marker may help in breast cancer diagnosis. HSP90AA1 is highly associated with various malignant tumors. In addition to breast cancer, HSP90AA1 is sensitive in lung cancer, and can be used as an initial diagnosis for hepatocellular tumors.

Many functional markers were included in the study and demonstrated a higher correlation with cancer than patients who are not. The association between high expression of HSP90 and a poor prognosis overall was particularly strong in women with large lymph nodes, tumors, and the degree of invasiveness. Additionally patients with high HSP90 levels had a lower outlook than those with low levels of expression of the gene.

The Boster Bio HSP90AB1 biomarker is an extremely sensitive blood test that detects the presence of HSP90 in plasma. It is highly specific and sensitive, and has the potential to be used as a test for the diagnosis of cancer. Although it is not clear whether this protein could be used as a marker of cancer however, it was recently found that the HSP90AB1 gene could be used to differentiate cancer patients from non-cancer patients.

The Boster Bio HSP90AB1 gene expression was linked to a poor prognosis for TNBC and HER2-/ER+ breast cancers. The subtypes with high levels of HSP90AB1 that is up-regulated, HSP90 expression was associated with a greater risk of distant metastasis as well as the possibility of recurrence.

The researchers have discovered that the Boster Bio HSP90AB1 signatures of genes are present in breast cancer tissues, and in the case of cancer that is recurrent, the expression is significantly higher than in healthy tissues. The study also found a link between the high HSP90AB1 expression and low overall survival. The HSP90AB1 gene, which is a HSP90 paralog, plays an important role folding proteins that are involved in secretory pathways, such as Toll-like receptors and integrins. This gene is associated with lower survival rates and an increased chance of recurrence of breast cancer.