抗HSP22抗体 | Anti-HSP22 antibody
掲載日情報:2018/10/03 現在Webページ番号:251745
StressMarq Biosciences社の抗HSP22抗体(Anti-HSP22 antibody)です。
※本製品は研究用です。研究用以外には使用できません。
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[在庫・価格 :2024年06月17日 00時00分現在]
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Anti-Hsp22, Mouse-Mono(3C12-H11) |
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本製品は取扱中止になりました | 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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[在庫・価格 :2024年06月17日 00時00分現在]
※ 表示されている納期は弊社に在庫が無く、取り寄せた場合の納期目安となります。
Anti-Hsp22, Mouse-Mono(3C12-H11)
文献数: 0
- 商品コード:SMC-187C
- メーカー:STQ
- 包装:25μg
- 本製品は取扱中止になりました
説明文 |
クローン:3C12-H11 Genbank No: 26353 Gene Accession No: NP_055180.1 Protein Accession No: Q9UJY1 |
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別包装品 | 別包装品あり | ||||||
法規制等 | |||||||
保存条件 | 法規備考 | ||||||
抗原種 | Human | 免疫動物 | Mouse | ||||
交差性 | Human/Mouse/Rat | 適用 | ELISA,IC,IF,IHC,Western Blot | ||||
標識 | Unlabeled | 性状 | Protein A/G Affinity Purified | ||||
吸収処理 | クラス | IgG | |||||
クロナリティ | Monoclonal | フォーマット | |||||
掲載カタログ |
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製品記事 |
抗HSP22抗体 | Anti-HSP22 antibody 熱ショックタンパク質研究用製品特集 神経科学(Neuroscience)研究用 抗体/タンパク質 (StressMarq Biosciences社) |
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製品情報
Product Name
HSP22 Antibody
Clonality
Monoclonal
Description
Mouse Anti-Human HSP22 Monoclonal IgG1 Kappa
Research Areas
Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Neurodegeneration, Neuroscience, Protein Trafficking
Alternative Names
Alpha crystallin C chain Antibody, CMT2L Antibody, CRYAC Antibody, DHMN2 Antibody, H11 Antibody, Heat shock 22kDa protein 8 Antibody, HMN2 Antibody, HSB8 Antibody, HSPB8 Antibody
Clone Number
3C12-H11
Host Species
Mouse
Isotype
IgG1 Kappa
Immunogen
His-tagged human recombinant HSP22
Applications
WB, IHC, ICC/IF, ELISA
Species Reactivity
Human, Mouse, Rat
Accession Number
NP_055180.1, NP_055180.2
Gene ID
26353, 26354
Swiss Prot
Q9UJY1, Q9UJY2
Specificity
Detects ~22kDa. Detects endogenous and exogenous HSP22 in monomeric, dimeric and tetrameric forms in WB. Does not cross react with alpha crystallin.
Purification
Protein G Purified
Storage Buffer
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Certificate of Analysis
1 µg/ml of SMC-187 was sufficient for detection of HSP22 in 20 µg of whole rat tissue extract by ECL immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
References
Scientific Background
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6).
References
1.Kappe G., et al. (2001) Biochem Biophys Acta 1520: 1-6.
2. Benndorf R., et al. (2001) J Biol Chem 276: 26753-26761.
3.Sun X., et al. (2004) J Biol Chem 279: 2394-2402.
4.Kim M.V., et al. (2004) Biochem Biophys Res Commun 325: 649-652.
5. Wilhelmus M.M., et al. (2006)Acta Neuropathol (Berl) 111: 139-149.
HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6).
References
1.Kappe G., et al. (2001) Biochem Biophys Acta 1520: 1-6.
2. Benndorf R., et al. (2001) J Biol Chem 276: 26753-26761.
3.Sun X., et al. (2004) J Biol Chem 279: 2394-2402.
4.Kim M.V., et al. (2004) Biochem Biophys Res Commun 325: 649-652.
5. Wilhelmus M.M., et al. (2006)Acta Neuropathol (Berl) 111: 139-149.
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