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Typical Testing Data/Standard Curve (for reference only)

Human Heat Shock 70kDa Protein 8 (HSPA8) RTU ELISA Kit | HSPA8 rtu elisa kit

Human Heat Shock 70kDa Protein 8 (HSPA8) ELISA Kit

Gene Names
HSPA8; LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
Reactivity
Human
Synonyms
Heat Shock 70kDa Protein 8 (HSPA8); Human Heat Shock 70kDa Protein 8 (HSPA8) ELISA Kit; LAP1; HSC54; HSC70; HSC71; HSP71; HSPA10; NIP71; HSP73; Heat shock cognate 71 kDa protein; Lipopolysaccharide-associated protein 1; LPS-associated protein 1; HSPA8 rtu elisa kit
Ordering
For Research Use Only!
Reactivity
Human
Sequence Length
646
Assay Type
Sandwich
Samples
Serum, Plasma, Tissue Homogenates or Other Biological Fluids.
Detection Range
0.312-20ng/mL
Sensitivity
0.134ng/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)

Typical Testing Data/Standard Curve (for reference only)
Related Product Information for HSPA8 rtu elisa kit
Test Principle: The microtiter plate provided in this kit has been pre-coated with an antibody specific to HSPA8. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to HSPA8. 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 HSPA8, 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 HSPA8 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 #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
53,518 Da
NCBI Official Full Name
heat shock cognate 71 kDa protein isoform 1
NCBI Official Synonym Full Names
heat shock protein family A (Hsp70) member 8
NCBI Official Symbol
HSPA8
NCBI Official Synonym Symbols
LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; LAP-1; NIP71; HEL-33; HSPA10; HEL-S-72p
NCBI Protein Information
heat shock cognate 71 kDa protein
UniProt Protein Name
Heat shock cognate 71 kDa protein
UniProt Gene Name
HSPA8
UniProt Synonym Gene Names
HSC70; HSP73; HSPA10; LAP-1; LPS-associated protein 1

NCBI Description

This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 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. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones 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:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).

Research Articles on HSPA8

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Product Notes

The Human HSPA8 hspa8 (Catalog #AAA459964) is a RTU ELISA Kit and is intended for research purposes only. The product is available for immediate purchase. The AAA459964 RTU ELISA Kit recognizes Human HSPA8. It is sometimes possible for the material contained within the vial of "Heat Shock 70kDa Protein 8 (HSPA8), RTU ELISA Kit" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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