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CRYAB Mouse anti-Human, Rat, Clone: OTI6D11, liquid, TrueMAB™

Mouse Monoclonal Antibody
Supplier: OriGene TA500583S

Description
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 maintece. Alpha-B crystallin has been linked to Alexander′s disease where it accumulates in brain cells of those afflicted.Specifications
CRYAB | |
Monoclonal | |
1 mg/mL | |
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide | |
P02511, P23928 | |
Cryab | |
Full length human recombit protein of human CRYAB produced in HEK293T cell. | |
30 μL | |
Primary | |
Human, Rat | |
Antibody | |
IgG1 |
Flow Cytometry, Immunocytochemistry, Immunofluorescence, Immunohistochemistry (Paraffin), Immunoprecipitation | |
OTI6D11 | |
Unconjugated | |
CRYAB | |
CMD1II, CRYA2, CTPP2, CTRCT16, HEL-S-101, HSPB5, MFM2 | |
Mouse | |
Affinity Chromatography | |
RUO | |
1410, 25420 | |
-20° C, Avoid Freeze/Thaw Cycles | |
Liquid |
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