Human Heat Shock 70kDa Protein 1B (HSPA1B) ELISA Kit | HSPA1B elisa kit

Human Heat Shock 70kDa Protein 1B (HSPA1B) ELISA Kit

Cat. Num. AAA2104781

• Gene Names: HSPA1B; HSP72; HSPA1; HSX70; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1B
• Reactivity: Human
• Synonyms: Heat Shock 70kDa Protein 1B (HSPA1B); Human Heat Shock 70kDa Protein 1B (HSPA1B) ELISA Kit; HSP70-2; HSP-A1B; Heat Shock Protein 72; HSPA1B elisa kit

• Reactivity: Human
• Specificity: This assay has high sensitivity and excellent specificity for detection of HSPA1B. No significant cross-reactivity or interference between HSPA1B and analogues was observed.
• Sequence Length: 641

• Application Notes: Enzyme-linked immunosorbent assay for Antigen Detection.
• Samples: Serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids
• Assay Type: Quantitative Sandwich
• Detection Range: 1.56-100ng/mL
• Sensitivity: < 0.61ng/mL
• Intra-assay Precision: Intra-assay Precision (Precision within an assay): 3 samples with low, middle and high level HSPA1B were tested 20 times on one plate, respectively. Intra-Assay: CV<10%
• Inter-assay Precision: Inter-assay Precision (Precision between assays): 3 samples with low, middle and high level HSPA1B were tested on 3 different plates, 8 replicates in each plate. CV(%) = SD/meanX100. Inter-Assay: CV<12%
• Preparation and Storage: The stability of kit is determined by the loss rate of activity. The loss rate of this kit is less than 5% within the expiration date under appropriate storage condition.; To minimize extra influence on the performance, operation procedures and lab conditions, especially room temperature, air humidity, incubator temperature should be strictly controlled. It is also strongly suggested that the whole assay is performed by the same operator from the beginning to the end.

Typical Testing Data/Standard Curve (for reference only)

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Related Product Information for HSPA1B elisa kit

Intended Uses: The kit is a sandwich enzyme immunoassay for in vitro quantitative measurement of HSPA1B in human serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Principle of the Assay: The microplate provided in this kit has been pre-coated with an antibody specific to HSPA1B. Standards or samples are then added to the appropriate microplate wells with a biotin-conjugated antibody specific to HSPA1B. 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 HSPA1B, 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 HSPA1B in the samples is then determined by comparing the O.D. of the samples to the standard curve.

Product Categories/Family for HSPA1B elisa kit

Infection immunity

NCBI and Uniprot Product Information

• NCBI GI #: 167466173
• NCBI GeneID: 3304
• NCBI Accession #: NP_005337.2
• NCBI GenBank Nucleotide #: NM_005346.5
• UniProt Accession #: P0DMV9; P08107; P19790; Q5JQI4; Q5SP17; Q9UQL9; Q9UQM0; B4E3B6
• Molecular Weight: 70,052 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1B
• NCBI Official Synonym Full Names: heat shock protein family A (Hsp70) member 1B
• NCBI Official Symbol: HSPA1B
• NCBI Official Synonym Symbols: HSP72; HSPA1; HSX70; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1B
• NCBI Protein Information: heat shock 70 kDa protein 1B
• UniProt Protein Name: Heat shock 70 kDa protein 1B
• Protein Family: Heat shock 70 kDa protein
• UniProt Gene Name: HSPA1B
• UniProt Synonym Gene Names: HSP721 PublicationManual assertion based on opinion iniRef.36; HSP70-22 PublicationsManual assertion based on opinion iniRef.3; HSP70.2

NCBI Description

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

Uniprot Description

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).