产品: | HSPA2 抗体 |
货号: | DF8101 |
描述: | Rabbit polyclonal antibody to HSPA2 |
应用: | WB IHC |
反应: | Human, Mouse, Monkey |
预测: | Pig, Bovine, Sheep, Rabbit, Dog |
分子量: | 70 kDa; 70kD(Calculated). |
蛋白号: | P54652 |
RRID: | AB_2841446 |
产品描述
*The optimal dilutions should be determined by the end user.
*Tips:
WB: 适用于变性蛋白样本的免疫印迹检测. IHC: 适用于组织样本的石蜡(IHC-p)或冰冻(IHC-f)切片样本的免疫组化/荧光检测. IF/ICC: 适用于细胞样本的荧光检测. ELISA(peptide): 适用于抗原肽的ELISA检测.
引用格式: Affinity Biosciences Cat# DF8101, RRID:AB_2841446.
展开/折叠
70kDa; Hcp70.2; Heat shock 70 kDa protein 2; Heat shock protein 2; Heat shock protein 70.2; Heat shock related 70 kDa protein 2; Heat shock-related 70 kDa protein 2; Heat-shock protein, 70-KD, 2; Heat-shock protein, 70-KD, 3; HSP70 2; HSP70 3; Hsp70-2; HSP70-3; HSP70.2; HSP70A2; HSP72; HSP72_HUMAN; HSPA2; Hspt70; Hst70; MGC58299; MGC7795; MGC93458; OTTHUMP00000180664; Testis-specific heat shock protein-related;
抗原和靶标
- P54652 HSP72_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGETKTFFPEEISSMVLTKMKEIAEAYLGGKVHSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPVEKALRDAKLDKGQIQEIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILIGDKSENVQDLLLLDVTPLSLGIETAGGVMTPLIKRNTTIPTKQTQTFTTYSDNQSSVLVQVYEGERAMTKDNNLLGKFDLTGIPPAPRGVPQIEVTFDIDANGILNVTAADKSTGKENKITITNDKGRLSKDDIDRMVQEAERYKSEDEANRDRVAAKNALESYTYNIKQTVEDEKLRGKISEQDKNKILDKCQEVINWLDRNQMAEKDEYEHKQKELERVCNPIISKLYQGGPGGGSGGGGSGASGGPTIEEVD
种属预测
score>80的预测可信度较高,可尝试用于WB检测。*预测模型主要基于免疫原序列比对,结果仅作参考,不作为质保凭据。
High(score>80) Medium(80>score>50) Low(score<50) No confidence
翻译修饰 - P54652 作为底物
Site | PTM Type | Enzyme | Source |
---|---|---|---|
Y16 | Phosphorylation | Uniprot | |
K26 | Ubiquitination | Uniprot | |
T38 | Phosphorylation | Uniprot | |
T39 | Phosphorylation | Uniprot | |
S41 | Phosphorylation | Uniprot | |
Y42 | Phosphorylation | Uniprot | |
T46 | Phosphorylation | Uniprot | |
T48 | Phosphorylation | Uniprot | |
R50 | Methylation | Uniprot | |
K57 | Acetylation | Uniprot | |
T65 | Phosphorylation | Uniprot | |
T67 | Phosphorylation | Uniprot | |
K72 | Acetylation | Uniprot | |
K78 | Ubiquitination | Uniprot | |
K101 | Ubiquitination | Uniprot | |
K103 | Ubiquitination | Uniprot | |
Y108 | Phosphorylation | Uniprot | |
K109 | Acetylation | Uniprot | |
K109 | Ubiquitination | Uniprot | |
T112 | Phosphorylation | Uniprot | |
K113 | Ubiquitination | Uniprot | |
S121 | Phosphorylation | Uniprot | |
S122 | Phosphorylation | Uniprot | |
T126 | Phosphorylation | Uniprot | |
T159 | Phosphorylation | Uniprot | |
T164 | Phosphorylation | Uniprot | |
T166 | Phosphorylation | Uniprot | |
T178 | Phosphorylation | Uniprot | |
Y184 | Phosphorylation | Uniprot | |
K188 | Acetylation | Uniprot | |
K188 | Ubiquitination | Uniprot | |
K189 | Ubiquitination | Uniprot | |
K223 | Ubiquitination | Uniprot | |
S224 | Phosphorylation | Uniprot | |
T225 | Phosphorylation | Uniprot | |
T229 | Phosphorylation | Uniprot | |
K249 | Acetylation | Uniprot | |
T268 | Phosphorylation | Uniprot | |
T276 | Phosphorylation | Uniprot | |
S280 | Phosphorylation | Uniprot | |
T301 | Phosphorylation | Uniprot | |
K322 | Acetylation | Uniprot | |
K328 | Ubiquitination | Uniprot | |
K348 | Ubiquitination | Uniprot | |
K351 | Acetylation | Uniprot | |
K351 | Ubiquitination | Uniprot | |
K360 | Acetylation | Uniprot | |
K360 | Sumoylation | Uniprot | |
K360 | Ubiquitination | Uniprot | |
K364 | Sumoylation | Uniprot | |
K364 | Ubiquitination | Uniprot | |
S365 | Phosphorylation | Uniprot | |
T421 | Phosphorylation | Uniprot | |
K454 | Acetylation | Uniprot | |
K454 | Ubiquitination | Uniprot | |
T465 | Phosphorylation | Uniprot | |
R472 | Methylation | Uniprot | |
T498 | Phosphorylation | Uniprot | |
K500 | Ubiquitination | Uniprot | |
K503 | Ubiquitination | Uniprot | |
T505 | Phosphorylation | Uniprot | |
K510 | Acetylation | Uniprot | |
K510 | Sumoylation | Uniprot | |
K510 | Ubiquitination | Uniprot | |
K515 | Acetylation | Uniprot | |
R520 | Methylation | Uniprot | |
R527 | Methylation | Uniprot | |
K564 | Methylation | Uniprot | |
T634 | Phosphorylation | Uniprot |
研究背景
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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity).
Cytoplasm>Cytoskeleton>Spindle.
Note: Colocalizes with SHCBP1L at spindle during the meiosis process.
Interacts with FKBP6. Interacts with ZNF541. Component of the CatSper complex. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2. Interacts with SHCBP1L; this interaction may promote the recruitment of HSPA2 to the spindle (By similarity). Interacts with FKBP6.
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.
研究领域
· 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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