Loading...
Loading...
Loading...
Loading...
Try browsing our complete catalog of products.
Cosmo Bio
Cosmo Bio
Neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.
Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found in 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 quotes disease where it accumulates in brain cells of those afflicted.
Western Blotting (WB):0.5 µg/ml
Immunofluorescence (IF):5 µg/ml
Immunohistochemistry (Paraffin) (IHC (P)): assay dependent
| Package Size | 50 µg |
|---|---|
| Form | Liquid (0.1M NaPB, pH7.0, 20 mg/ml BSA, 0.1% Sodium Azide (NaN3) added) |
| Concentration | 1 mg/mL |
| Purity | Affinity Purified |
| Host | Rabbit Polyclonal |
| Immunogen | Synthetic phosphopeptide corresponding to residues F(54)LRAPS(p)WIDTG(64) of human alpha-B Crystallin |
| Specificity | Alpha-B crystallin p59S |
| Cross Reactivity | Bovine, Human, Rat |
| Subclass | IgG |
| Storage | Store below -20°C. Avoid freeze-thaw cycles. |
1) Ito H, Okamoto K, Nakayama H, Isobe T, Kato K. (1997) Phosphorylation of B-crystallin in response to various types of stress. J Biol Chem. 272, 29934-29941.
2) Kato K, Ito H, Kamei K, Inaguma Y, Iwamoto I, Saga S. (1998) Phosphorylation of B-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem. 273, 28346-28354.
3) Ito H, Iida K, Kamei K, Iwamoto I, Inaguma Y, Kato K. (1999) B-crystallin in rat lens is phosphorylated at an early postnatal age. FEBS Lett. 446, 269-272.
| Product Specifications | |
| Application | IF, IHC(p), WB |
| Reactivity | Bovine, Human, Rat |
| Clonality | Polyclonal |
| Host | Rabbit |
| Documents & Links for Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) | |
| Datasheet | Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) Datasheet |
| Documents & Links for Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) | |
| Datasheet | Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) Datasheet |
Neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease have been increasing rapidly and have become a serious social problem. In recent years, new causative genes have been discovered for amyotrophic lateral sclerosis (ALS) and other intractable neurological diseases opening new avenues for research on pathogenesis. It has been suggested that aggregation and accumulation of specific proteins cause neurotoxicity and the formation of lesions, but the onset and progression mechanisms are still unclear. Neuropathological diagnostic and experimental model biomarkers are needed for drug construction, drug discovery, and therapeutic development.
Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found in 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 quotes disease where it accumulates in brain cells of those afflicted.
Western Blotting (WB):0.5 µg/ml
Immunofluorescence (IF):5 µg/ml
Immunohistochemistry (Paraffin) (IHC (P)): assay dependent
| Package Size | 50 µg |
|---|---|
| Form | Liquid (0.1M NaPB, pH7.0, 20 mg/ml BSA, 0.1% Sodium Azide (NaN3) added) |
| Concentration | 1 mg/mL |
| Purity | Affinity Purified |
| Host | Rabbit Polyclonal |
| Immunogen | Synthetic phosphopeptide corresponding to residues F(54)LRAPS(p)WIDTG(64) of human alpha-B Crystallin |
| Specificity | Alpha-B crystallin p59S |
| Cross Reactivity | Bovine, Human, Rat |
| Subclass | IgG |
| Storage | Store below -20°C. Avoid freeze-thaw cycles. |
1) Ito H, Okamoto K, Nakayama H, Isobe T, Kato K. (1997) Phosphorylation of B-crystallin in response to various types of stress. J Biol Chem. 272, 29934-29941.
2) Kato K, Ito H, Kamei K, Inaguma Y, Iwamoto I, Saga S. (1998) Phosphorylation of B-crystallin in mitotic cells and identification of enzymatic activities responsible for phosphorylation. J Biol Chem. 273, 28346-28354.
3) Ito H, Iida K, Kamei K, Iwamoto I, Inaguma Y, Kato K. (1999) B-crystallin in rat lens is phosphorylated at an early postnatal age. FEBS Lett. 446, 269-272.
| Product Specifications | |
| Application | IF, IHC(p), WB |
| Reactivity | Bovine, Human, Rat |
| Clonality | Polyclonal |
| Host | Rabbit |
| Documents & Links for Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) | |
| Datasheet | Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) Datasheet |
| Documents & Links for Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) | |
| Datasheet | Anti Alpha-Crystallin B Chain, p59S pAb (Rabbit, Affinity Purified) Datasheet |
No reviews have been added for this product.