Thermo Fisher Scientific CRYAB Monoclonal Antibody (1D11C6E6)

Applications

Tested Dilution

Publications

Western Blot (WB)

1:500-1:2,000

-

Immunohistochemistry (Paraffin) (IHC (P))

1:200-1:1,000

-

Immunocytochemistry (ICC/IF)

-

View 1 publication 1 publication

ELISA (ELISA)

1:10,000

-

Product Specifications

Species Reactivity

Human

Published species

Human

Host/Isotype

Mouse / IgG2a

Class

Monoclonal

Type

Antibody

Clone

1D11C6E6

Immunogen

Purified recombinant fragment of CRYAB (aa1-175) expressed in E. Coli. if (typeof window.$mangular === undefined || !window.$mangular) { window.$mangular = {}; } $mangular.antigenJson = \[{targetFamily:CRYAB,uniProtId:P02511-1,ncbiNodeId:9606,antigenRange:1-175,antigenLength:175,antigenImageFileName:MA5-15383_CRYAB_P02511-1_House_mouse.svg,antigenImageFileNamePDP:MA5-15383_CRYAB_P02511-1_House_mouse_PDP.jpeg,sortOrder:1}\]; $mangular.isB2BCMGT = false; $mangular.isEpitopesModalImageMultiSizeEnabled = true;

View immunogen .st0{fill:#FFFFFF;} .st1{fill:#1E8AE7;}

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

Conc. Not Determined

Storage buffer

ascites

Contains

0.03% sodium azide

Storage conditions

Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.

Shipping conditions

Wet ice

RRID

AB_10974499

Product Specific Information

MA5-15383 targets CRYAB in indirect ELISA, IHC and WB applications and shows reactivity with Human samples.

The MA5-15383 immunogen is purified recombinant fragment of CRYAB (aa1-175) expressed in E. Coli.

Target Information

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`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.