抗FKBP51抗体 | Anti-FKBP51 antibody
掲載日情報:2018/10/03 現在Webページ番号:251718
StressMarq Biosciences社の抗FKBP51抗体(Anti-FKBP51 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06月25日 20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-FKBP51, Hi51B, Monoclonal |
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本製品は取扱中止になりました | 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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[在庫・価格 :2024年06月25日 20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-FKBP51, Hi51B, Monoclonal
文献数: 1
- 商品コード:SMC-138C
- 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:Hi51B Genbank No: 2289 Gene Accession No: NP_001139247.1 Protein Accession No: Q13451 |
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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 | Dog/Hamster/Human/Mouse/Rabbit/Rat | 適用 | IC,IF,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FKBP51モノクローナル抗体(Anti-FKBP51) FKBP51 antibody (Hi51B:クローン名) | StressMarq Biosciences 抗FKBP51抗体 | Anti-FKBP51 antibody |
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製品情報
Product Name
FKBP51 Antibody
Clonality
Monoclonal
Description
Mouse Anti-Human FKBP51 Monoclonal IgG
Research Areas
Cancer, Heat Shock, Cell Signaling, Nuclear Import/Export, Protein Trafficking
Alternative Names
AIG6 Antibody, FK506 binding protein 5 Antibody, FKBP5 Antibody, FKBP54 Antibody, HSP90 binding immunophilin Antibody, p54 Antibody, Pplase Antibody, Ptg10 Antibody, Rotamase Antibody, T cekk FK506 binding protein Antibody
Clone Number
Hi51B
Host Species
Mouse
Isotype
IgG
Immunogen
Synthetic peptide corresponding to the residues of human FKBP51
Applications
WB, ICC/IF
Species Reactivity
Dog, Human, Mouse, Rat, Hamster, Rabbit
Accession Number
NP_001139247.1
Gene ID
2289
Swiss Prot
Q13451
Specificity
Detects ~51kDa.
Purification
Protein G Purified
Storage Buffer
PBS, 50% glycerol, 0.09% sodium azide
Certificate of Analysis
A 1:2000 dilution was sufficient for detection of FKBP51 in ~50 µg total protein using WB analysis.
References
Scientific Background
HSP90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more cochaperones (1). One class of HSP90-binding cochaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an HSP90 binding site. Among the TPR cochaperones of HSP90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins (2). FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex (3). The N terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPIase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TPR repeats involved in protein-protein interactions with the HSP90 (4). Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different HSP90-binding characteristics (3). FK506 binding protein 51 kDa (FKBP51 or otherwise referred to as FKBP54) has been identified as a progestininducible gene. This protein is predominantly expressed in murine T cells but in humans, it is abundantly expressed in numerous tissues at levels many times higher than FKBP12. The FKBP51 gene is known to be induced by glucocorticoids (5).
References
1. Cheung-Flynn J., Roberts P.J., Riggs D.L., and Smith D.F.(2003) J. Biol. Chem. 278(19): 17388-17394.
2. Davies T.H., Ning Y.N., and Sanchez E.R. (2002) J Biol. Chem. 277 (7): 4597-4600.
3. Wu B. et al. (2004) Proc. Natl. Acad. Sci. USA. 101(22): 8348-8353.
4. Denny W.B., Prapapanich V., Smith D.F., and Scammell J.G. (2005) Endocrinology 146(7): 3194-3201.
5. Hubler T.R. et al. (2003) Endocrinology 144(6): 2380- 2387.
HSP90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more cochaperones (1). One class of HSP90-binding cochaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an HSP90 binding site. Among the TPR cochaperones of HSP90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins (2). FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex (3). The N terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPIase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TPR repeats involved in protein-protein interactions with the HSP90 (4). Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different HSP90-binding characteristics (3). FK506 binding protein 51 kDa (FKBP51 or otherwise referred to as FKBP54) has been identified as a progestininducible gene. This protein is predominantly expressed in murine T cells but in humans, it is abundantly expressed in numerous tissues at levels many times higher than FKBP12. The FKBP51 gene is known to be induced by glucocorticoids (5).
References
1. Cheung-Flynn J., Roberts P.J., Riggs D.L., and Smith D.F.(2003) J. Biol. Chem. 278(19): 17388-17394.
2. Davies T.H., Ning Y.N., and Sanchez E.R. (2002) J Biol. Chem. 277 (7): 4597-4600.
3. Wu B. et al. (2004) Proc. Natl. Acad. Sci. USA. 101(22): 8348-8353.
4. Denny W.B., Prapapanich V., Smith D.F., and Scammell J.G. (2005) Endocrinology 146(7): 3194-3201.
5. Hubler T.R. et al. (2003) Endocrinology 144(6): 2380- 2387.
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