Application Note: Anti-Crystallin Alpha B Antibody is suitable for use in WB, IHC and IF microscopy. Expect a band approximately ~22kDa on specific lysates. Specific conditions for reactivity should be optimized by the end user.
Concentration Value: 85 mg/mL
Immunohistochemistry Dilution: User Optimized
Western Blot Dilution: 1:5000-10000
General Disclaimer Note: This product is for research use only and is not intended for therapeutic or diagnostic applications. Please contact a technical service representative for more information. All products of animal origin manufactured by Rockland Immunochemicals are derived from starting materials of North American origin. Collection was performed in United States Department of Agriculture (USDA) inspected facilities and all materials have been inspected and certified to be free of disease and suitable for exportation. All properties listed are typical characteristics and are not specifications. All suggestions and data are offered in good faith but without guarantee as conditions and methods of use of our products are beyond our control. All claims must be made within 30 days following the date of delivery. The prospective user must determine the suitability of our materials before adopting them on a commercial scale. Suggested uses of our products are not recommendations to use our products in violation of any patent or as a license under any patent of Rockland Immunochemicals, Inc. If you require a commercial license to use this material and do not have one, then return this material, unopened to: Rockland Inc., P.O. BOX 5199, Limerick, Pennsylvania, USA.
Immunogen: Crystallin Alpha B Antibody was produced from whole rabbit serum prepared by repeated immunizations with a synthetic peptide corresponding to human alpha B crystallin.
Physical State: Liquid (sterile filtered)
Purity and Specificity: Anti-Crystallin Alpha B Antibody was prepared from monospecific antiserum by delipidation and defibrination. A BLAST analysis was used to suggest cross-reactivity with Crystallin Alpha B from Human, Mouse, Rat, Cow, and Chicken based on 100% homology with the immunizing sequence. Does not cross-react with α A-crystallin. Cross-reactivity with Crystallin Alpha B from other sources has not been determined. Heat Shock research.
Background: The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess structural and functional similarities with Hsp25 and Hsp27. Mammalian lens cystallins are divided into alpha, beta and gamma families. Alpha and beta families are further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the lens, alpha-crystallin primarily functions to maintain proper refractive index, however it can also function as a molecular chaperone that binds to the denatured proteins, keeping them in solution and thereby maintaining the translucency of the lens. When cellular stress occurs, alpha-crystallin enters its’ phosphorylated state and may serve a structural control function and play a role in protein maintenance. In addition to their interaction with proteins, alpha-crystallins also interact with native molecules such as membrane proteins, Golgi matrix protein, structural proteins, nuclear proteins and DNA. Two other functions are an autokinase activity and participation in the intracellular architecture, and it has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases. Specifically, alpha-B cystallin is found in many cells and organs outside the lens, and alpha B is overexpressed in several neurological disorders and in cell lines under stress conditions.
Low Endotoxin: No
English
Deutsch
