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CRYAB Mouse anti-Human, Clone: OTI3E3, liquid, TrueMAB™
SDP

Mouse Monoclonal Antibody

Supplier:  OriGene TA500580

Encompass_Preferred

Catalog No. 50-167-1719


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Description

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

Specifications

CRYAB
Monoclonal
0.9 mg/mL
PBS with 1% BSA, 50% glycerol and 0.02% sodium azide
P02511
CRYAB
Full length human recombit protein of human CRYAB produced in HEK293T cell.
100 μL
Primary
Human
Antibody
IgG1
Immunocytochemistry, Immunofluorescence, Immunoprecipitation, Western Blot
OTI3E3
Unconjugated
CRYAB
CMD1II, CRYA2, CTPP2, CTRCT16, HEL-S-101, HSPB5, MFM2
Mouse
Affinity Chromatography
RUO
1410
-20° C, Avoid Freeze/Thaw Cycles
Liquid
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