Anti-ALDH3A1 Magnetic Beads-IP Kit Product Components
Components | Storage |
Anti-ALDH3A1 Magnetic Beads1,3 | 2-8℃ for 12 months |
NP40 Cell Lysis Buffer2 | -20℃ for 12 months |
5×TBST(pH7.4) | |
1×TBST(pH7.4) | |
ddH2O | |
CD166 Positive Cell Lysate | -20℃ for 12 months |
Alkaline Elution Buffer | 2-8℃ for 12 months |
Acidity Elution Buffer | 2-8℃ for 12 months |
Neutralization Buffer | 2-8℃ for 12 months |
[1] The IP KIT contains anti-ALDH3A1 magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).
[2] Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.
[3] Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.
Anti-ALDH3A1 Magnetic Beads-IP Kit Product Description
The Anti-ALDH3A1 magnetic Beads, conjugated with Anti-ALDH3A1 antibody, are used for immuneprecipitation (IP) of ALDH3A1 proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing ALDH3A1 proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound ALDH3A1 proteins are dissociated from the magnetic beads using an elution buffer. Anti-ALDH3A1 Magnetic Beads-IP Kit Antibody Information
Immunogen
Recombinant Human ALDH3A1 protein (Catalog#12523-H07B)
Species Reactivity
Human ALDH3A1
Source
Polyclonal Human Rabbit IgG
Preparation
Produced in rabbits immunized with purified, recombinant Human ALDH3A1 (rh ALDH3A1; Catalog#12523-H07B; AAH04370.1; Met1-His453). ALDH3A1 specific IgG was purified by Human ALDH3A1 affinity chromatography.
Applications
Immunoprecipitation (IP), Minimum Protein Purification
Anti-ALDH3A1 Magnetic Beads Immunoprecipitation (IP) Kit Alternative Names
Anti-ALDH3ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit;Anti-ALDHIIIALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit
ALDH3A1 Background Information
Aldehyde dehydrogenase 3A1 (ALDH3A1) is a metabolic enzyme that catalyzes the oxidation of various aldehydes. Certain types of epithelial tissues in mammals, especially those continually exposed to environmental stress (e.g., corneal epithelium), express ALDH3A1 at high levels and its abundance in such tissues is perceived to help to maintain cellular homeostasis under conditions of oxidative stress. Metabolic as well as non-metabolic roles for ALDH3A1 have been associated with its mediated resistance to cellular oxidative stress. Aldehyde dehydrogenase 1A1 (ALDH1A1) and ALDH3A1 are corneal crystallins. They protect inner ocular tissues from ultraviolet radiation (UVR)-induced oxidative damage through catalytic and non-catalytic mechanisms. Additionally, ALDH3A1 has been postulated to play a regulatory role in the corneal epithelium based on several studies that report an inverse association between ALDH3A1 expression and corneal cell proliferation. Aldehyde dehydrogenase 3A1 (ALDH3A1) plays an important role in many cellular oxidative processes, including cancer chemoresistance, by metabolizing activated forms of oxazaphosphorine drugs such as cyclophosphamide (CP) and its analogues, such as mafosfamide (MF), ifosfamide (IFM), and 4-hydroperoxycyclophosphamide (4-HPCP). Compounds that can selectively target ALDH3A1 could permit delineation of its roles in these processes and could restore chemosensitivity in cancer cells that express this isoenzyme. ALDH3A1 may act to protect corneal cells against cellular oxidative damage by metabolizing toxic lipid peroxidation products (e.g., 4-HNE), maintaining cellular GSH levels and redox balance, and operating as an antioxidant.
Full Name
aldehyde dehydrogenase 3 family, member A1
References
Pappa A, et al. (2003) Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea. Biochem J. 376(3): 615-23. Estey T, et al. (2007) ALDH3A1: a corneal crystallin with diverse functions. Experimental Eye Research. 84(1):3-12. Pappa A, et al. (2003) Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage. Free Radical Biology and Medicine. 34(9):1178-89.