|Tested species reactivity||Bovine, Human, Mouse, Rat|
|Published species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phopshopeptide corresponding to residues L(44) S(p) P F Y L R P P S F(54) C of human alpha-B Crystallin.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 30mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunofluorescence (IF)||5 ug/ml|
|Immunohistochemistry (Paraffin) (IHC (P))||8 ug/ml|
|Western Blot (WB)||0.5 ug/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA1-011 detects phospho-alpha-B crystallin (Ser45) from bovine, human, mouse and rat samples. This antibody does not detect the unphosphorylated form of the protein.
PA1-011 has been successfully used in Western blot, immunohistochemistry and immunofluorescence procedures. By Western blot, this antibody detects an ~20 kDa protein representing recombinant bovine phospho-alpha-B crystallin (Ser45). Immunofluorescence staining of phospho-alpha-B crystallin (Ser45) in U373 MG cells results in cytoplasmic staining.
The PA1-011 immunogen is a synthetic phopshopeptide corresponding to residues L(44) S(p) P F Y L R P P S F(54) C of human alpha-B Crystallin.
Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products--alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens.
Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander and quote;s disease where it accumulates in brain cells of those afflicted.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Hyperglycemia induced expression, phosphorylation, and translocation of ¿B-crystallin in rat skeletal muscle.
PA1-011 was used in immunohistochemistry - paraffin section and western blot to study the role of alphaBC under chronic hyperglycemia in rat skeletal muscle
|Reddy VS,Jakhotia S,Reddy PY,Reddy GB||IUBMB life (67:291)||2015|
Expression and induction of small heat shock proteins in rat heart under chronic hyperglycemic conditions.
PA1-011 was used in western blot to examine the expression of sHsp under chronic hyperglycemic conditions in rat heart
|Reddy VS,Kumar ChU,Raghu G,Reddy GB||Archives of biochemistry and biophysics (558:1)||2014|
O-GlcNAcylation of ¿B-crystallin regulates its stress-induced translocation and cytoprotection.
PA1-011 was used in western blot to study the role of alphaB-crystallin O-GlcNAcylation in regulating its translocation in response to stress and its cytoprotective effects in cardiomyocytes
|Krishnamoorthy V,Donofrio AJ,Martin JL||Molecular and cellular biochemistry (379:59)||2013|