抗HO-1抗体 | Anti-HO-1 antibody
掲載日情報：2018/10/03 現在Webページ番号：251712
StressMarq Biosciences社の抗HO-1抗体(Anti-HO-1 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-HO-1, Mouse-Mono(1F12-A6) |
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本製品は取扱中止になりました | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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[在庫・価格 ：2025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-HO-1, Mouse-Mono(1F12-A6)
文献数： 4
- 商品コード：SMC-131C
- 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：1F12-A6 Genbank No： 3162 Gene Accession No： NP_002124.1 Protein Accession No： P09601 |
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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 | Bovine/Dog/Guinea Pig/Hamster/Human/Monkey/Mouse/Pig/Rabbit/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 | |||||
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| 製品記事 | 抗HO-1抗体 | Anti-HO-1 antibody 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-HO-1 Monoclonal Antibody, Clone 1F12-A6 (SMC-131). Tissue: HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-HO-1 Monoclonal Antibody (SMC-131) 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: Microsome. Endoplasmic reticulum. Localizaes to the nucleus upon hypoxia. Magnification: 100x. (A) DAPI (blue) nuclear stain. (B) Anti-HO-1 Antibody. (C) Composite. |
 | Immunohistochemistry analysis using Mouse Anti-HO-1 Monoclonal Antibody, Clone 1F12-A6 (SMC-131). Tissue: backskin. Species: Mouse. Fixation: Bouin’s Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-HO-1 Monoclonal Antibody (SMC-131) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: muscle, dermis, hair follicles, epidermis: nuclear everywhere and some cytoplasmic staining. |
 | Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-HO-1 Monoclonal Antibody, Clone 1F12-A6 (SMC-131). Tissue: HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Mouse Anti-HO-1 Monoclonal Antibody (SMC-131) at 1:100 for 12 hours at 4°C. Secondary Antibody: R-PE Goat Anti-Mouse (yellow) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Microsome. Endoplasmic reticulum. Localizaes to the nucleus upon hypoxia. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-HO-1 Antibody. (C) Composite. |
 | Western Blot analysis of Human HeLa cell lysates showing detection of HO-1 protein using Mouse Anti-HO-1 Monoclonal Antibody, Clone 1F12-A6 (SMC-131). Load: 15 µg protein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-HO-1 Monoclonal Antibody (SMC-131) 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-HO-1 Monoclonal Antibody, Clone 1F12-A6 (SMC-131). Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20°C. Primary Antibody: Mouse Anti-HO-1 Monoclonal Antibody (SMC-131) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Cellcell border staining in epidermis, punctuate nuclear staining. . |
Product Name
HO-1 Antibody
Clonality
Monoclonal
Description
Mouse Anti-Human HO-1 Monoclonal IgG1 Kappa
Research Areas
Cancer, Alzheimer's Disease, Atherosclerosis, Blood, Cancer Metabolism, Cardiovascular System, Cell Signaling, Endothelium, Epigenetics and Nuclear Signaling, Hypoxia, Inflammatory Mediators, Metabolism, Metabolism processes, Neurodegeneration, Neuroscience, NFkB Pathway, Nuclear Signaling Pathways, Oxidative Stress, Platelets, Response to Hypoxia, Vascular Inflammation, Vasculature
Alternative Names
HSP32 Antibody, HMOX1 Antibody, Heme oxygenase 1 Antibody, HO Antibody, HO1 Antibody
Clone Number
1F12-A6
Host Species
Mouse
Isotype
IgG1 Kappa
Immunogen
Human HO-1 synthetic peptide, amino acids 1-30
Applications
WB, IHC, ICC/IF, IP, ELISA
Species Reactivity
Dog, Human, Monkey, Mouse, Rat, Bovine, Guinea Pig (Cavia porcellus), Hamster, Pig, Rabbit
Accession Number
NP_002124.1
Gene ID
3162
Swiss Prot
P09601
Specificity
Detects 32kDa. Does not cross-react with HO-2.
Purification
Protein G Purified
Storage Buffer
PBS pH7.4, 50% glycerol, 0.09% sodium azide
Certificate of Analysis
1 µg/ml was sufficient for detection of HO-1 in 10 µg of mixed human cell line lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
References
Scientific Background
Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin (1). These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs (2). There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals (3). HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
References
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86.
2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47.
3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411–419.
4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8.
5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 10925–10930.
6. Yet S.F., et al. (2003) FASEB J. 17: 1759–1761.
7. Yachie A., et al. (1999) J Clin Invest. 103: 129–135.
Heme-oxygenase is a ubiquitous enzyme that catalyzes the initial and rate-limiting steps in heme catabolism yielding equimolar amounts of biliverdin, iron and carbon monoxide. Biliverdin is subsequently converted to bilirubin and the free iron is sequestered to ferritin (1). These products have important physiological effects as carbon monoxide is a potent vasodilator; biliverdin and bilirubin are potent antioxidants; and the free iron increases oxidative stress and regulates the expression of many mRNAs (2). There are three isoforms of heme-oxygenase, HO-1, HO-2 and HO-3; however HO-1 and HO-2 are the major isoforms as they both have been identified in mammals (3). HO-1, also known as heat shock protein 32, is an inducible isoform activated by most oxidative stress inducers, cytokines, inflammatory agents and heat shock. HO-2 is a constitutive isoform which is expressed under homeostatic conditions. HO-1 is also considered to be a cytoprotective factor in that free heme is highly reactive and cytotoxic, and secondly, carbon monoxide is a mediator inhibiting the inflammatory process and bilirubin is a scavenger for reactive oxygen, both of which are the end products of heme catalyzation (4). It has also been shown that HO-1 deficiency may cause reduced stress defense, a pro-inflammatory tendency (5), susceptibility to atherosclerotic lesion formation (6), endothelial cell injury, and growth retardation (7). Up-regulation of HO-1 is therefore said to be one of the major defense mechanisms of oxidative stress (4).
References
1. Froh M. et al. (2007) World J. Gastroentereol 13(25): 3478-86.
2. Elbirt K.K. and Bonkovsky H.L. (1999) Proc Assoc Am Physicians 111(5): 348-47.
3. Maines M.D., Trakshel G.M., and Kutty R.K. (1986) J Biol Chem 261: 411–419.
4. Brydun A., et al. (2007) Hypertens Res 30(4): 341-8.
5. Poss K.D. and Tonegawa S. (1997). Proc Natl Acad Sci U S A. 94: 10925–10930.
6. Yet S.F., et al. (2003) FASEB J. 17: 1759–1761.
7. Yachie A., et al. (1999) J Clin Invest. 103: 129–135.
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