抗Grp75抗体 | Anti-Grp75 antibody
掲載日情報：2018/10/03 現在Webページ番号：251713
StressMarq Biosciences社の抗Grp75抗体(Anti-Grp75 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 ：2025年04月26日 08時35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-Grp75, Mouse-Mono(S52A-42) |
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本製品は取扱中止になりました | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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[在庫・価格 ：2025年04月26日 08時35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-Grp75, Mouse-Mono(S52A-42)
文献数： 5
- 商品コード：SMC-133C
- 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：S52A-42 Genbank No： 3313 Gene Accession No： NP_004125.3 Protein Accession No： P38646 |
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| 法規制等 | |||
| 保存条件 | 法規備考 | ||
| 抗原種 | Mouse | 免疫動物 | Mouse |
| 交差性 | C. elegans/Human/Mouse/Rat | 適用 | ELISA,IC,IF,IHC,IP,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Grp75抗体 | Anti-Grp75 antibody 神経変性（Neurodegeneration）関連抗体（StressMarq Biosciences社） 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
 | Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Grp75 Monoclonal Antibody, Clone S52A-42 (SMC-133). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Grp75 Monoclonal Antibody (SMC-133) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Mitochondria. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-Grp75 Antibody. (C) Composite. |
 | Western Blot analysis of Human HeLa cell lysates showing detection of Grp75 protein using Mouse Anti-Grp75 Monoclonal Antibody, Clone S52A-42 (SMC-133). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Grp75 Monoclonal Antibody (SMC-133) at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT. |
 | Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Grp75 Monoclonal Antibody, Clone S52A-42 (SMC-133). Tissue: Heat Shocked HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-Grp75 Monoclonal Antibody (SMC-133) at 1:100 for 12 hours at 4°C. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Mitochondria. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-Grp75 Antibody. (C) Composite. |
Product Name
Grp75 Antibody
Clonality
Monoclonal
Description
Mouse Anti-Mouse Grp75 Monoclonal IgG1
Research Areas
Cancer, Heat Shock, Alzheimer's Disease, Cell Cycle, Cell Division, Cell Signaling, Chaperone Proteins, Metabolism, Mitochondrial Markers, Mitochondrial Metabolism, Neurodegeneration, Neuroscience, Parkinson's Disease, Protein Trafficking, Tumor Biomarkers
Alternative Names
HSC74 Antibody, HSP74 Antibody, HSPA9 Antibody, HSPa9a Antibody, HSPA9B Antibody, Mortalin 2 Antibody, MOT2 Antibody, PBP74 Antibody
Clone Number
S52A-42
Host Species
Mouse
Isotype
IgG1
Immunogen
Fusion protein amino acids 551-766 of mouse SALM2.
Applications
WB, IHC, ICC/IF, IP, ELISA
Species Reactivity
Human, Mouse, Rat, Nematode (Caenorhabditis elegans)
Accession Number
NP_004125.3
Gene ID
3313
Swiss Prot
P38646
Specificity
Detects ~75kDa.
Purification
Protein G Purified
Storage Buffer
PBS pH7.2, 50% glycerol, 0.09% sodium azide
Certificate of Analysis
1 µg/ml was sufficient for detection of Grp75 in 10 µg of heat shock HeLa lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
References
Scientific Background
Grp75, also known as mortalin, is a member of HSP70 family of chaperone proteins that is not heat inducible (1, 2). Grp75 is actually induced under conditions of low glucose and other nutritional and environmental stresses. Grp75 resides primarily in the mitochondrial matrix, where it collaborates with HSP60 in the re-folding of proteins translocated into this organelle (3, 4). Related forms may also be found in the cytosol or on the surface of the extracellular membrane. Other Grp75 functions include its ability to inactivate the tumor suppressor p53 (5). Studies have found that Grp75 is over-expressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (6). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (7). And finally, like its E.coli homolog DnaK (8), GRP75 possesses a cation-dependent ATPase activity considered central to its function as a chaperone (9, 10).
References
1. Kaul S.C., et al. (1993) Biochem Biophys Res Commun. 193: 348-355.
2. Wadhwa R., et al. (1993) J Biol Chem 268: 6615-6621.
3. Schneider H.C., et al. (1994) Nature 371: 768-774.
4. Manning-Krieg U.C., et al. (1991) EMBO J. 10: 3273-3280.
5. Wadhwa R., et al. (1998) J Biol Chem. 273: 29586-91.
6. Wadhwa R., et al. (2006) Int J Cancer 118: 2973-2980.
7. Kaul S.C., et al. (2003) Exp Cell Res. 286: 96-110.
8. Liberek K., et al. (1991) J Biol Chem. 266: 14491-14496.
9. Mizzen L.A., et al. (1991) Cell Regulation. 2: 165-179.
10. Leustek U.K., et al. (1989) PNAS USA. 86: 7805-7808.
Grp75, also known as mortalin, is a member of HSP70 family of chaperone proteins that is not heat inducible (1, 2). Grp75 is actually induced under conditions of low glucose and other nutritional and environmental stresses. Grp75 resides primarily in the mitochondrial matrix, where it collaborates with HSP60 in the re-folding of proteins translocated into this organelle (3, 4). Related forms may also be found in the cytosol or on the surface of the extracellular membrane. Other Grp75 functions include its ability to inactivate the tumor suppressor p53 (5). Studies have found that Grp75 is over-expressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (6). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (7). And finally, like its E.coli homolog DnaK (8), GRP75 possesses a cation-dependent ATPase activity considered central to its function as a chaperone (9, 10).
References
1. Kaul S.C., et al. (1993) Biochem Biophys Res Commun. 193: 348-355.
2. Wadhwa R., et al. (1993) J Biol Chem 268: 6615-6621.
3. Schneider H.C., et al. (1994) Nature 371: 768-774.
4. Manning-Krieg U.C., et al. (1991) EMBO J. 10: 3273-3280.
5. Wadhwa R., et al. (1998) J Biol Chem. 273: 29586-91.
6. Wadhwa R., et al. (2006) Int J Cancer 118: 2973-2980.
7. Kaul S.C., et al. (2003) Exp Cell Res. 286: 96-110.
8. Liberek K., et al. (1991) J Biol Chem. 266: 14491-14496.
9. Mizzen L.A., et al. (1991) Cell Regulation. 2: 165-179.
10. Leustek U.K., et al. (1989) PNAS USA. 86: 7805-7808.
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