抗HSP40, YDJ1抗体 | Anti-HSP40, YDJ1 antibody
掲載日情報：2018/10/03 現在Webページ番号：251732
StressMarq Biosciences社の抗HSP40, YDJ1抗体(Anti-HSP40, YDJ1 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05月04日 13時55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-Hsp40, Ydj1, Mouse-Mono(2A7.H6) |
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本製品は取扱中止になりました | 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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[在庫・価格 ：2024年05月04日 13時55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-Hsp40, Ydj1, Mouse-Mono(2A7.H6)
文献数： 2
- 商品コード：SMC-166C
- 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：2A7.H6 Genbank No： 855661 Gene Accession No： NP_014335.1 Protein Accession No： P25491 |
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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 | Yeast | 免疫動物 | Mouse | ||||
| 交差性 | Yeast | 適用 | Western Blot,IP,ELISA | ||||
| 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 |
HSP(Heat Shock Protein)関連抗体 抗HSP40, YDJ1抗体 | Anti-HSP40, YDJ1 antibody 熱ショックタンパク質研究用製品特集 |
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製品情報
 | Western Blot analysis of Yeast recombinant cell lysate showing detection of Hsp40 protein using Mouse Anti-Hsp40 Monoclonal Antibody, Clone 2A7.H6 (SMC-166). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp40 Monoclonal Antibody (SMC-166) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT. |
Product Name
HSP40, YDJ1 Antibody
Clonality
Monoclonal
Description
Mouse Anti-Yeast HSP40, YDJ1 Monoclonal IgG1 Kappa
Research Areas
Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Protein Trafficking
Alternative Names
DnaJ (HSP40) homolog subfmaily B member 1 antibody, DNAJ 1 antibody, DNAJ B1 antibody, DnaJ homolog subfamily B member 1 antibody, DnaJ protein homolog 1 antibody, DNAJ1 antibody, DNAJB 1 antibody, DNAJB1 antibody, DNAJB1 protein antibody, DNJB1_HUMAN antibody, HDJ 1 antibody, HDJ-1 antibody, HDJ1 antibody, Heat shock 40 kDa protein 1 antibody, Heat shock 40kD protein 1 antibody, Heat shock protein 40 antibody, HSP 40 antibody, HSP40 antibody, HSPF 1 antibody, HSPF1 antibody, Human DnaJ protein 1 antibody, Radial spoke 16 homolog B antibody, RSPH16B antibody, Sis1 antibody
Clone Number
2A7.H6
Host Species
Mouse
Isotype
IgG1 Kappa
Immunogen
Full length protein HSP40 (YDJ1)
Applications
WB, IP, ELISA
Species Reactivity
Yeast
Accession Number
NP_014335.1
Gene ID
855661
Swiss Prot
P25491
Specificity
Detects ~40kDa. Yeast specific. Does not cross react with Human, Mouse or Rat.
Purification
Protein G Purified
Storage Buffer
50% glycerol, 0.09% sodium azide
Certificate of Analysis
0.5 µg/ml of SMC-166 was sufficient for detection of 50 ng YDJ1 by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
References
Scientific Background
Human HSP40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein) (1). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain (2). Members of the HSP40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. In particular, Hdj1, the first human HSP40/DnaJ protein identified, plays an important role in protein translation and folding, as well as in the regulation of HSP70 function (3). HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins (4, 5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 which leads to protein folding, or components of protein degradation machinery CHIP and BAG-1 (6). Some studies have shown that the difference between HDJ1 and type 1 DNAJ proteins including HDJ2 and yeast YdjI is the result of the possession of a zinc finger domain by the latter, which helps in the function of protein folding. (7, 8).
References
1. Cheetham M.E. and Caplan A.J. (1998) Cell Stress Chaperones 3: 28–36.
2. Fan C.Y., et al. (2003) Cell Stress Chaperones 8: 309–316.
3. Sohn S.Y., Kim S.B., Kim J., and Ahn B.Y. (2006) J Gen Virol. 87(7): 1883-91.
4. Liberek K. et al. (1991) Proc. Natl. Acad. Sci. USA 88: 2874–2878.
5. Cyr D.M., et al. (1992) J Biol Chem. 267: 20927–20931.
6. Höhfeld J., et al. (2001) EMBO Rep. 2: 885–890.
7. Terda K., et al. (1997) J Cell Biol. 139: 1089-1095.
8. Lu Z. and Cyr D.M. (1998) J Biol Chem. 273: 27824-27830.
Human HSP40/DnaJ proteins comprise a large protein family, members of which feature the J domain (named after the bacterial DnaJ protein) (1). The J-domain spans the first 75 N-terminal amino acids and is separated from the C-terminal by a glycine/phenylalanine-rich domain (2). Members of the HSP40/DnaJ family play diverse roles in many cellular processes, such as folding, translocation, degradation and assembly of multi-protein complexes. In particular, Hdj1, the first human HSP40/DnaJ protein identified, plays an important role in protein translation and folding, as well as in the regulation of HSP70 function (3). HSP40 stimulates the ATPase activity of HSP70 which in turn causes conformational changes of the unfolded proteins (4, 5). The HSP40-HSP70-unfolded protein complex further binds to co-chaperones Hip, Hop and HSP90 which leads to protein folding, or components of protein degradation machinery CHIP and BAG-1 (6). Some studies have shown that the difference between HDJ1 and type 1 DNAJ proteins including HDJ2 and yeast YdjI is the result of the possession of a zinc finger domain by the latter, which helps in the function of protein folding. (7, 8).
References
1. Cheetham M.E. and Caplan A.J. (1998) Cell Stress Chaperones 3: 28–36.
2. Fan C.Y., et al. (2003) Cell Stress Chaperones 8: 309–316.
3. Sohn S.Y., Kim S.B., Kim J., and Ahn B.Y. (2006) J Gen Virol. 87(7): 1883-91.
4. Liberek K. et al. (1991) Proc. Natl. Acad. Sci. USA 88: 2874–2878.
5. Cyr D.M., et al. (1992) J Biol Chem. 267: 20927–20931.
6. Höhfeld J., et al. (2001) EMBO Rep. 2: 885–890.
7. Terda K., et al. (1997) J Cell Biol. 139: 1089-1095.
8. Lu Z. and Cyr D.M. (1998) J Biol Chem. 273: 27824-27830.
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