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Каталожный номерHY029014
Описание
Anti-HSPA1A Polyclonal Antibody (HY029014) is a rabbit polyclonal antibody detecting HSPA1A in ELISA, IHC, WB. Suitable for Human, Mouse, Rat, Bovine, and Bos mutus grunniens.
Highlights
  • ●Affinity Purified — Minimal background and high purity for reliable results.
  • ●Multi-Application — Validated across multiple applications.
  • ●Multi-Species — Cross-reactive for translational research.
Реактивность видовHuman, Mouse, Rat
ПримененияELISA, IHC, WB
Хозяинский видRabbit
КлоональностьPolyclonal
ИзотипIgG
Иммуноген E. coli - derived recombinant Human HSPA1A (Met1-Asp641).
Цель HSP70.1, HSP70-1, HSPA1, HSPA1A, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1, HSP72, HSX70
Очистка Purified by antigen affinity column.
Номер доступа P0DMV8
Форма Liquid
Буфер хранения 0.01M PBS, pH 7.4, 50% Glycerol, 0.05% Proclin 300.

Пожалуйста, обратитесь к конкретной информации о буфере в печатной версии даташита или в индивидуальном сертификате качества (COA) для партии.

Информация об использовании продукта
Применение Разбавление
ELISA 1:5000-1:20000
IHC 1:50-1:500
WB 1:500-1:2000
Устойчивость и хранение Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt.
Фон

Heat shock 70 kDa protein 1A (HSPA1A) is a ~70 kDa protein. 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.

1. Mayer, MP. (2013) Trends in biochemical sciences 38, 507-14. PMID: 24012426
2. Rauch, JN. et al. (2014) The Journal of biological chemistry 289, 1402-14. PMID: 24318877
3. Radons, J. (2016) Cell stress & chaperones 21, 379-404. PMID: 26865365
4. Seo, JH. et al. (2016) Nature communications 7, 12882. PMID: 27708256
5. Fang, CT. et al. (2016) Cellular and molecular life sciences : CMLS 73, 3949-60. PMID: 27137183
6. Shang, Y. et al. (2014) Biochemical and biophysical research communications 446, 387-92. PMID: 24613385
7. Chen, Z. et al. (2013) Immunity 39, 272-85. PMID: 23973223
8. Shi, Y. et al. (1998) Genes & development 12, 654-66. PMID: 9499401
9. Wang, WF. et al. (2017) Nature communications 8, 363. PMID: 28842558
Примечание For research use only.
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Formula
Mass (g) = Concentration (mol/L) × Volume (L) × MW (g/mol)
Enter any 2 of Mass, Concentration, Volume + Molecular Weight to solve for the unknown.
Mass
=
Concentration
×
Volume
Molecular Weight *
g/mol
Formula
C₁ × V₁ = C₂ × V₂
Enter any 3 of the 4 values to solve for the unknown.
Stock Solution
C₁ (Stock Conc.)
×
V₁ (Stock Vol.)
=
Working Solution
C₂ (Working Conc.)
×
V₂ (Working Vol.)
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