bs-17708R [Primary Antibody]
Rabbit  Anti-HSPB4/Alpha A Crystallin  Polyclonal Antibody
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Host: Rabbit

Target Protein: HSPB4/Alpha A Crystallin

IR: Immunogen Range:81-173/173

Clonality: Polyclonal

Isotype: IgG

Entrez Gene: 1409

Swiss Prot: P02489

Source: KLH conjugated synthetic peptide derived from human HSPB4/Alpha A Crystallin:81-173/173 

Purification: affinity purified by Protein A

Storage: 0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol. Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.

Background: Mammalian lens crystallins are divided into alpha, beta, and gamma families. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC). [provided by RefSeq, Jan 2014]

Size: 200ul

Concentration: 1mg/ml

Applications: IHC-P=1:100-500, IHC-F=1:100-500, ICC=1:100-500, IF=1:100-500, ELISA=1:5000-10000

Cross Reactive Species: (predicted: Human,Mouse,Rat,Dog,Pig,Cow,Rabbit,Sheep)

For research use only. Not intended for diagnostic or therapeutic use.

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