抗HSC70 (plant)抗体 | Anti-HSC70 (plant) antibody
掲載日情報：2018/10/03 現在Webページ番号：26536
StressMarq Biosciences社の抗HSC70 (plant)抗体(Anti-HSC70 (plant) 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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価格
[在庫・価格 ：2024年04月30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。
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Anti-Hsc70(plant), Rabbit-Poly |
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[在庫・価格 ：2024年04月30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-Hsc70(plant), Rabbit-Poly
文献数： 0
- 商品コード：SPC-302D
- メーカー：STQ
- 包装：100μl
- 本製品は取扱中止になりました
| 説明文 | |||
|---|---|---|---|
| 法規制等 | |||
| 保存条件 | 法規備考 | ||
| 抗原種 | Plant | 免疫動物 | Rabbit |
| 交差性 | Plant | 適用 | ELISA,IP,Western Blot |
| 標識 | Unlabeled | 性状 | Serum |
| 吸収処理 | クラス | ||
| クロナリティ | Polyclonal | フォーマット | |
| 掲載カタログ |
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| 製品記事 |
植物由来Hsp関連抗体 |
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| 関連記事 | |||
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製品情報
Product Name
HSC70 (plant) Antibody
Clonality
Polyclonal
Description
Rabbit Anti-Plant HSC70 (plant) Polyclonal
Research Areas
Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Protein Trafficking, Tumor Biomarkers
Alternative Names
HSP70 1 Antibody, HSP70 2 Antibody, HSP70.1 Antibody, HSP72 Antibody, HSPA1 Antibody, HSPA1A Antibody, HSPA1B Antibody, HSPA8 Antibody
Host Species
Rabbit
Immunogen
HSC70 purified from wheat germ
Applications
WB, ELISA, IP
Species Reactivity
Pea (Pisum sativum), Plant, Wheat (Triticum spp.)
Specificity
Detects ~70kDa.
Purification
Rabbit antiserum
Storage Buffer
Lyophilized rabbit Antiserum. For reconstitution add 100 µl of sterile water.
References
Scientific Background
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (5).
References
1. Boorstein W.R., Ziegelhoffer T., and Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17.
2. Rothman J. (1989) Cell 59: 591-601.
3. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
4. Bork P., Sander C., and Valencia A. (1992) Proc. Natl Acad. Sci. USA 89: 7290-7294.
5. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833-840.
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (5).
References
1. Boorstein W.R., Ziegelhoffer T., and Craig E.A. (1993) J. Mol. Evol. 38(1): 1-17.
2. Rothman J. (1989) Cell 59: 591-601.
3. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
4. Bork P., Sander C., and Valencia A. (1992) Proc. Natl Acad. Sci. USA 89: 7290-7294.
5. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833-840.
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