ELISA/assay

Bovine Heat Shock 70kDa Protein 1A ELISA Kit

MBS736390

48-Strip-Wells

470 USD

ELISA Kit

Bovine Heat Shock 70kDa Protein 1A ELISA Kit

Heat Shock 70kDa Protein 1A

heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1A/1B; heat shock 70 kDa protein 1A/1B; HSP70-1/HSP70-2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70 kDa protein 1/2; epididymis secretory protein Li 103; dnaK-type molecular chaperone HSP70-1; heat shock 70kDa protein 1A; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSPA1A

HSPA1A; HSPA1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-1A; HEL-S-103; HSPA1; HSX70 HSPA1B ; HSP70-1/HSP70-2; HSP70.1/HSP70.2

HSP71_HUMAN

Bovine

This assay has high sensitivity and excellent specificity for detection of HSP70k1A. No significant cross-reactivity or interference between HSP70k1A and analogues was observed. NOTE: Limited by current skills and knowledge, it is impossible for us to complete the cross-reactivity detection between HSP70k1A and all the analogues, therefore, cross reaction may still exist in some cases.

Store all reagents at 2-8 degree C.

Samples: Serum, plasma, Cell Culture Supernatants, body fluid and tissue homogenate. Assay Type: Sandwich. Sensitivity: 1.0 ng/mL.

Intended Uses: This HSP70k1A ELISA kit is a 1.5 hour solid-phase ELISA designed for the quantitative determination of Bovine HSP70k1A. This ELISA kit for research use only, not for therapeutic or diagnostic applications!

Signal Transduction

Principle of the assay: HSP70k1A ELISA kit applies the quantitative sandwich enzyme immunoassay technique. The microtiter plate has been pre-coated with a monoclonal antibody specific for HSP70k1A. Standards or samples are then added to the microtiter plate wells and HSP70k1A if present, will bind to the antibody pre-coated wells. In order to quantitatively determine the amount of HSP70k1A present in the sample, a standardized preparation of horseradish peroxidase (HRP)-conjugated polyclonal antibody, specific for HSP70k1A are added to each well to "sandwich" the HSP70k1A immobilized on the plate. The microtiter plate undergoes incubation, and then the wells are thoroughly washed to remove all unbound components. Next, substrate solutions are added to each well. The enzyme (HRP) and substrate are allowed to react over a short incubation period. Only those wells that contain HSP70k1A and enzyme-conjugated antibody will exhibit a change in color. The enzyme-substrate reaction is terminated by addition of a sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450 nm. A standard curve is plotted relating the intensity of the color (O.D.) to the concentration of standards. The HSP70k1A concentration in each sample is interpolated from this standard curve.

194248072

NP_005336.3

NM_005345.5

63,937 Da

Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Apoptosis Modulation By HSP70 Pathway (198877); Direct P53 Effectors Pathway (137939); Endocytosis Pathway (102279); Endocytosis Pathway (102181); Epstein-Barr Virus Infection Pathway (585562); Epstein-Barr Virus Infection Pathway (587115); Estrogen Signaling Pathway (799177); Estrogen Signaling Pathway (799197)

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]

HSP70: a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Protein type: Heat shock protein; Motility/polarity/chemotaxis; Chaperone. Chromosomal Location of Human Ortholog: 6p21.3. Cellular Component: signalosome; focal adhesion; mitochondrion; endoplasmic reticulum; inclusion body; ribonucleoprotein complex; cytosol; centriole; nucleoplasm; perinuclear region of cytoplasm; cytoplasm; nuclear speck; nucleus; vesicle; ubiquitin ligase complex. Molecular Function: viral receptor activity; protein binding; enzyme binding; G-protein-coupled receptor binding; ubiquitin protein ligase binding; heat shock protein binding; ATPase activity; unfolded protein binding; double-stranded RNA binding; protein N-terminus binding; ATPase activity, coupled; ATP binding. Biological Process: negative regulation of cell proliferation; entry of virus into host cell; protein stabilization; positive regulation of erythrocyte differentiation; mRNA catabolic process; negative regulation of protein ubiquitination; protein refolding; gene expression; negative regulation of cell growth; response to unfolded protein; negative regulation of apoptosis

48-Strip-Wells

470 USD

96-Strip-Wells

675