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ELK Biotechnology
SKU:ES9136
CRYAA rabbit pAb
CRYAA rabbit pAb
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$250.00 USD
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Applications: WB;ELISA
Reactivity: Human;Mouse;Rat
Source: Rabbit
Dilution: WB 1:500-2000 ELISA 1:5000-20000
Immunogen: Synthesized peptide derived from human protein . at AA range: 1-80
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Observed_band(KD): 19kD
Human_gene_id: 1409
Human_swiss_prot_no: P02489
Subcellular_location: Cytoplasm . Nucleus . Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
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 distin
Reactivity: Human;Mouse;Rat
Source: Rabbit
Dilution: WB 1:500-2000 ELISA 1:5000-20000
Immunogen: Synthesized peptide derived from human protein . at AA range: 1-80
Storage_stability: -20°C/1 year
Clonality: Polyclonal
Isotype: IgG
Concentration: 1 mg/ml
Observed_band(KD): 19kD
Human_gene_id: 1409
Human_swiss_prot_no: P02489
Subcellular_location: Cytoplasm . Nucleus . Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
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 distin
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