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Human Aldo-keto Reductase 1C1/AKR1C1 MAb (Clone 859026)  25 UG图1

Human Aldo-keto Reductase 1C1/AKR1C1 MAb (Clone 859026) 25 UG

2024-11-26 18:10IP属地 广东省东莞市 电信00留言

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Western Blot      
     

Detection of Human Aldo‑keto Reductase 1C1/AKR1C1 by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line and human liver tissue. PVDF membrane was probed with 0.1 µg/mL of Mouse Anti-Human Aldo‑keto Reductase 1C1/AKR1C1 Monoclonal Antibody (Catalog # MAB6529) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # ). A specific band was detected for Aldo‑keto Reductase 1C1/AKR1C1 at approximately 37 kDa (as indicated). This experiment was conducted under reducing conditions and using .

Simple Western      
     

Detection of Human Aldo‑keto Reductase 1C1/AKR1C1 by Simple WesternTM. Simple Western lane view shows lysates of HepG2 human hepatocellular carcinoma cell line and human liver tissue, loaded at 0.5 mg/mL. A specific band was detected for Aldo‑keto Reductase 1C1/AKR1C1 at approximately 41 kDa (as indicated) using 1 µg/mL of Mouse Anti-Human Aldo‑keto Reductase 1C1/AKR1C1 Monoclonal Antibody (Catalog # MAB6529). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.


Preparation and Storage

Background: Aldo-keto Reductase 1C1/AKR1C1

AKR1C1 (20-alpha -hydroxysteroid dehydrogenase, 20‑ alpha ‑HSD) is a member of aldo-keto reductase (AKR) superfamily. AKRs perform the NAD(P)H-dependent reduction of carbonyl groups (1). Four AKR1C isoforms (AKR1C1-C4) are known to exist in humans. They are all highly expressed in the liver. Three isoforms, excluding AKR1C4, have a wider expression pattern including prostate, testes, uterus, mammary gland, and haemopoietic progenitors (2). These enzymes are able to accept various natural steroids as substrates, including 3-, 7-, and 20‑ketosteroids (3). They can also activate prodrugs such as synthetic steroid hormone tibolone by converting it into active 3 alpha / beta -hydroxy form (4). They are recognized as phase I drug-metabolizing enzymes involved in the maintenance of steroid homeostasis, prostaglandin metabolism, and metabolic activation of polycyclic aromatic hydrocarbons (5). Their reactions introduce a hydroxyl group into the product making it available for sulfonation and glucuronidation by phase II enzyme. Elevated expression of these enzymes is related to cancer with hormone-dependent malignancies (6, 7). Increased levels of expression of AKR1C1 parallels increased cell proliferation activity in human colon cancer cells. It has been shown to be associated with oncogenic potential and proproliferative effects. It is also involved in cancer cell chemoresistance.

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