HSP77/76 Antibody - #DF2504
製品説明
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
引用形式: Affinity Biosciences Cat# DF2504, RRID:AB_2839710.
折りたたみ/展開
Heat shock 70 kDa protein B; Heat shock 70kDa protein 7 (HSP70B); HSP70B; Putative heat shock 70 kDa protein 7; Heat shock 70 kDa protein 6; Heat shock 70 kDa protein B'; Heat shock 70 kDa protein B''; heat shock 70kD protein 6 (HSP70B'); Heat shock 70kDa protein 6; HSP70B'; HSP70B-Prime; HSP76_HUMAN; HSPA6; OTTHUMP00000032372;
免疫原
- P48741 HSP77_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFQVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPTYFSNSQRQATKDAGAIAGLKVLPIINEATAAAIAYGLDRRGAGKRNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTPSSSTQATLEIDSLFEGVDFYKSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDFVLGGGLHSHPQGAEVAAGLLQRQGAEQEHQP
- P17066 HSP76_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MQAPRELAVGIDLGTTYSCVGVFQQGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPHNTVFDAKRLIGRKFADTTVQSDMKHWPFRVVSEGGKPKVRVCYRGEDKTFYPEEISSMVLSKMKETAEAYLGQPVKHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLSIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHGKDLSGNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDVVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVFIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGKANKITITNDKGRLSKEEVERMVHEAEQYKAEDEAQRDRVAAKNSLEAHVFHVKGSLQEESLRDKIPEEDRRKMQDKCREVLAWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGGPGVPGGSSCGTQARQGDPSTGPIIEEVD
PTMs - P48741/P17066 基板として
Site | PTM Type | Enzyme | Source |
---|---|---|---|
T39 | Phosphorylation | Uniprot | |
T40 | Phosphorylation | Uniprot | |
S42 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
T47 | Phosphorylation | Uniprot | |
T49 | Phosphorylation | Uniprot | |
R51 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S59 | Phosphorylation | Uniprot | |
K73 | Ubiquitination | Uniprot | |
K79 | Ubiquitination | Uniprot | |
K102 | Ubiquitination | Uniprot | |
K104 | Ubiquitination | Uniprot | |
K114 | Ubiquitination | Uniprot | |
S123 | Phosphorylation | Uniprot | |
K128 | Ubiquitination | Uniprot | |
K130 | Ubiquitination | Uniprot | |
T224 | Phosphorylation | Uniprot | |
K259 | Ubiquitination | Uniprot | |
T267 | Phosphorylation | Uniprot | |
S309 | Phosphorylation | Uniprot | |
S314 | Phosphorylation | Uniprot | |
T315 | Phosphorylation | Uniprot | |
K321 | Acetylation | Uniprot | |
K321 | Ubiquitination | Uniprot | |
K327 | Ubiquitination | Uniprot |
Site | PTM Type | Enzyme | Source |
---|---|---|---|
T39 | Phosphorylation | Uniprot | |
T40 | Phosphorylation | Uniprot | |
S42 | Phosphorylation | Uniprot | |
Y43 | Phosphorylation | Uniprot | |
T47 | Phosphorylation | Uniprot | |
T49 | Phosphorylation | Uniprot | |
R51 | Methylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
S59 | Phosphorylation | Uniprot | |
K73 | Ubiquitination | Uniprot | |
K79 | Ubiquitination | Uniprot | |
K90 | Ubiquitination | Uniprot | |
K102 | Ubiquitination | Uniprot | |
K104 | Ubiquitination | Uniprot | |
K114 | Ubiquitination | Uniprot | |
S123 | Phosphorylation | Uniprot | |
K128 | Ubiquitination | Uniprot | |
K130 | Ubiquitination | Uniprot | |
K142 | Methylation | Uniprot | |
K142 | Ubiquitination | Uniprot | |
K161 | Ubiquitination | Uniprot | |
Y185 | Phosphorylation | Uniprot | |
T224 | Phosphorylation | Uniprot | |
K259 | Ubiquitination | Uniprot | |
T267 | Phosphorylation | Uniprot | |
S278 | Phosphorylation | Uniprot | |
S298 | Phosphorylation | Uniprot | |
T300 | Phosphorylation | Uniprot | |
S309 | Phosphorylation | Uniprot | |
S314 | Phosphorylation | Uniprot | |
T315 | Phosphorylation | Uniprot | |
K321 | Acetylation | Uniprot | |
K321 | Ubiquitination | Uniprot | |
K327 | Ubiquitination | Uniprot | |
K330 | Methylation | Uniprot | |
K330 | Ubiquitination | Uniprot | |
K347 | Ubiquitination | Uniprot | |
K350 | Ubiquitination | Uniprot | |
K359 | Acetylation | Uniprot | |
K359 | Sumoylation | Uniprot | |
K359 | Ubiquitination | Uniprot | |
K363 | Sumoylation | Uniprot | |
K363 | Ubiquitination | Uniprot | |
S364 | Phosphorylation | Uniprot | |
Y373 | Phosphorylation | Uniprot | |
K386 | Ubiquitination | Uniprot | |
S402 | Phosphorylation | Uniprot | |
T407 | Phosphorylation | Uniprot | |
K453 | Ubiquitination | Uniprot | |
R460 | Methylation | Uniprot | |
R471 | Methylation | Uniprot | |
R495 | Methylation | Uniprot | |
K499 | Ubiquitination | Uniprot | |
K502 | Acetylation | Uniprot | |
K502 | Ubiquitination | Uniprot | |
T504 | Phosphorylation | Uniprot | |
K509 | Acetylation | Uniprot | |
K509 | Sumoylation | Uniprot | |
K509 | Ubiquitination | Uniprot | |
K514 | Ubiquitination | Uniprot | |
K528 | Ubiquitination | Uniprot | |
K541 | Ubiquitination | Uniprot | |
K552 | Ubiquitination | Uniprot | |
K563 | Methylation | Uniprot | |
K563 | Ubiquitination | Uniprot | |
K598 | Ubiquitination | Uniprot |
研究背景
Belongs to the heat shock protein 70 family.
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 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 N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.
Belongs to the heat shock protein 70 family.
研究領域
· Cellular Processes > Transport and catabolism > Endocytosis. (View pathway)
· Environmental Information Processing > Signal transduction > MAPK signaling pathway. (View pathway)
· Genetic Information Processing > Transcription > Spliceosome.
· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum. (View pathway)
· Human Diseases > Infectious diseases: Bacterial > Legionellosis.
· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.
· Human Diseases > Infectious diseases: Viral > Measles.
· Human Diseases > Infectious diseases: Viral > Influenza A.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Organismal Systems > Aging > Longevity regulating pathway - multiple species. (View pathway)
· Organismal Systems > Immune system > Antigen processing and presentation. (View pathway)
· Organismal Systems > Endocrine system > Estrogen signaling pathway. (View pathway)
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