Human Heat Shock Protein 90kDa Alpha B1 (HSP90aB1) RTU ELISA Kit | HSP90aB1 rtu elisa kit

Human Heat Shock Protein 90kDa Alpha B1 (HSP90aB1) ELISA Kit

Cat. Num. AAA459946

• Gene Names: HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B
• Reactivity: Human
• Synonyms: Heat Shock Protein 90kDa Alpha B1 (HSP90aB1); Human Heat Shock Protein 90kDa Alpha B1 (HSP90aB1) ELISA Kit; HSP90-BETA; HSP90B; HSPC2; HSPCB; HSP84; Heat Shock 90kD Protein 1; Beta; Heat shock 84 kDa; HSP90aB1 rtu elisa kit

• Reactivity: Human
• Sequence Length: 724

• Assay Type: Sandwich
• Samples: Serum, Plasma, Tissue Homogenates, Cell Lysates, Cell Culture Supernates or Other Biological Fluids.
• Detection Range: 1.56-100ng/mL
• Sensitivity: 0.67ng/mL
• RTU ELISA Kit's Advantage: The Ready-To-Use (RTU) Kits require fewer steps in setup and take less time to run. Detection Solutions are pre-diluted and total incubation time is shorter than many other ELISA Kits.
• Preparation and Storage: For unopened kits: All the reagents should be kept at 4 degree C upon receipt.; For opened kits: Once the kit is opened, the remaining reagents still need to be stored according to the above storage conditions. In addition, return the unused wells to the foil pouch containing the desiccant pack and reseal along entire edge of zip-seal.

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for HSP90aB1 rtu elisa kit

Test Principle: The microtiter plate provided in this kit has been pre-coated with an antibody specific to HSP90aB1. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to HSP90aB1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain HSP90aB1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of HSP90aB1 in the samples is then determined by comparing the O.D. of the samples to the standard curve.

NCBI and Uniprot Product Information

• NCBI GI #: 431822401
• NCBI GeneID: 3326
• NCBI Accession #: NP_001258898.1
• NCBI GenBank Nucleotide #: NM_001271969.1
• UniProt Accession #: P08238; Q5T9W7; Q9NQW0; Q9NTK6; B2R5P0
• Molecular Weight: 83,264 Da
• NCBI Official Full Name: heat shock protein HSP 90-beta isoform a
• NCBI Official Synonym Full Names: heat shock protein 90 alpha family class B member 1
• NCBI Official Symbol: HSP90AB1
• NCBI Official Synonym Symbols: HSP84; HSPC2; HSPCB; D6S182; HSP90B
• NCBI Protein Information: heat shock protein HSP 90-beta
• UniProt Protein Name: Heat shock protein HSP 90-beta
• Protein Family: Heat shock protein
• UniProt Gene Name: HSP90AB1
• UniProt Synonym Gene Names: HSP90B; HSPC2; HSPCB; HSP 90; HSP 84; HSP84

NCBI Description

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]

Uniprot Description

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked 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 modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).