癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
Rabbit Anti-Heme Oxygenase Polyclonal Antibody
Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, IHC-F, IF, E |
|---|---|
| Primary Accession | P09601 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 32819 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human HO-1 |
| Epitope Specificity | 101-200/288 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Microsome. Endoplasmic reticulum. |
| SIMILARITY | Belongs to the heme oxygenase family. |
| DISEASE | Defects in HMOX1 are the cause of heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]. A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | The hemeoxygenase-1 calls that the hemoglobin oxidizes to synthesize the enzyme again-1( hemeoxygenase-1, HO-1) is the catalyst enzyme that a kind of hemoglobin declines the solution, under the NADPH and the cell dye P-450 revivification enzymes and the member oxygen functions, the catalyst HO-1 hemoglobin declines the solution as the courage green vegetable, CO and irons, the former revivification has the very strong anti- to oxidize the ability after become the red vegetable of courage , the latter is a kind of important letter to make the member. |
| Gene ID | 3162 |
|---|---|
| Other Names | HO-1; HSP32; HMOX1D; bK286B1; Heme oxygenase 1; HMOX1; HO; HO1 |
| Target/Specificity | Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level). |
| Dilution | WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ELISA=1:5000-10000 |
| Format | 0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
| Name | HMOX1 |
|---|---|
| Synonyms | HO, HO1 |
| Function | [Heme oxygenase 1]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707). |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass type IV membrane protein; Cytoplasmic side |
| Tissue Location | Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level) |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.
REFERENCES
Yoshida T.,et al.Eur. J. Biochem. 171:457-461(1988).
Collins J.E.,et al.Genome Biol. 5:R84.1-R84.11(2004).
Dunham I.,et al.Nature 402:489-495(1999).
Keyse S.M.,et al.Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989).
Shibahara S.,et al.Eur. J. Biochem. 179:557-563(1989).
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