抗HIF1 alpha抗体 | Anti-HIF1 alpha antibody
掲載日情報:2018/10/03 現在Webページ番号:251743
StressMarq Biosciences社の抗HIF1 alpha抗体(Anti-HIF1 alpha 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11日 00時00分現在]
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Anti-HIF1α, Mouse-Mono(ESEE122) |
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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06月11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-HIF1α, Mouse-Mono(ESEE122)
文献数: 2
- 商品コード:SMC-184C
- 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:ESEE122 Genbank No: 15251 Gene Accession No: NP_034561.2 Protein Accession No: Q61221 |
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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 | Mouse | 免疫動物 | Mouse | ||||
交差性 | Bovine/Human/Mouse/Rat | 適用 | IC,IF,IHC,Western Blot,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 |
抗HIF1 alpha抗体 | Anti-HIF1 alpha antibody |
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関連記事 |
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製品情報
Product Name
HIF1 alpha Antibody
Clonality
Monoclonal
Description
Mouse Anti-Mouse HIF1 alpha Monoclonal IgG1
Research Areas
Cancer, Cell Signaling, Epigenetics and Nuclear Signaling, Oxidative Stress
Alternative Names
ARNT interacting protein Antibody, HIF1A Antibody, Hypoxia inducible factor 1 alpha Antibody, MOP1 Antibody, PASD8 Antibody
Clone Number
ESEE122
Host Species
Mouse
Isotype
IgG1
Immunogen
Recombinant fragment corresponding to amino acids 329-530
Applications
WB, IHC, ICC/IF, ELISA
Species Reactivity
Human, Mouse, Rat, Bovine
Accession Number
NP_034561.2
Gene ID
15251
Swiss Prot
Q61221
Specificity
Detects ~116kDa. Specific for HIF1Alpha.
Purification
Protein G Purified
Storage Buffer
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Certificate of Analysis
1 µg/ml of SMC-184 was sufficient for detection of HIF1α in 20 µg of CoCl2-induced Hela cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
References
Scientific Background
Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response of hypoxia (1). The HIF1 complex consists of two subunits, HIF1-Alpha and HIF1-Beta, which are basic helix-loop-helix proteins of the PAS family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VLH) E3 ligase complex; ubiquitination and proteasomal degradation follows (3, 4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).
References
1. Sharp F.R. and Bernaudin M. (2004) Nat Rev Neurosci 5: 437-48.
2. Wang G.L., et al. (1995) Proc Natl Acad Sci U S A 92: 5510-4.
3. Jaakkola P., et al. (2001) Science 292: 468-72.
4. Maxwell P.H., et al. (1999) Nature 399: 271-5.
5. Fukuda R., et al. (2002) J Biol Chem 277: 38205-11.
6. Jiang B.H., et al. (2001) Cell Growth Differ 12: 363-9.
7. Laughner E., et al. (2001) Mol Cell Biol 21: 3995-4004.
Hypoxia-inducible factor 1 (HIF1) is a heterodimeric transcription factor that plays a critical role in the cellular response of hypoxia (1). The HIF1 complex consists of two subunits, HIF1-Alpha and HIF1-Beta, which are basic helix-loop-helix proteins of the PAS family (2). HIF1 regulates the transcription of a broad range of genes that facilitate responses to the hypoxic environment, including genes regulating angiogenesis, erythropoiesis, cell cycle, metabolism and apoptosis. The widely expressed HIF-1α is typically degraded rapidly in normoxic cells by the ubiquitin/proteasomal pathway. Under normoxic conditions, HIF-1α is proline hydroxylated leading to a conformational change that promotes binding to the von Hippel Lindau protein (VLH) E3 ligase complex; ubiquitination and proteasomal degradation follows (3, 4). Both hypoxic conditions and chemical hydroxylase inhibitors (such as desferrioxamine and cobalt) inhibit HIF-1α degradation and lead to its stabilization. In addition, HIF-1α can be induced in an oxygen-independent manner by various cytokines through the PI3K-AKT-mTOR pathway (5-7).
References
1. Sharp F.R. and Bernaudin M. (2004) Nat Rev Neurosci 5: 437-48.
2. Wang G.L., et al. (1995) Proc Natl Acad Sci U S A 92: 5510-4.
3. Jaakkola P., et al. (2001) Science 292: 468-72.
4. Maxwell P.H., et al. (1999) Nature 399: 271-5.
5. Fukuda R., et al. (2002) J Biol Chem 277: 38205-11.
6. Jiang B.H., et al. (2001) Cell Growth Differ 12: 363-9.
7. Laughner E., et al. (2001) Mol Cell Biol 21: 3995-4004.
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