Crystallin Alpha B
Antibody: CPTC-CRYAB-1
Background
Catalog Number:
CPTC-CRYAB-1
Target Antigen:
Crystallin Alpha B
Isotype:
IgG2a
Species:
Mouse
Last Updated:
08/27/2009
Purchase
- Purchase CPTC-CRYAB-1 (CRYAB-1) - DSHB
Characterization Data [Compare Characterization Data]
Western Blot
Click to enlarge
Western Blot using CPTC-CRYAB-1 as primary Ab against Ag 10408 (lane 2). Also included are molecular wt. standards (lane 1) and mouse IgG control (lane 3).
Characterization SOP Files
Indirect ELISA
Click to enlarge
Indirect ELISA (ie, binding of Antibody to Antigen coated plate)
Characterization SOP Files
Antibody: CPTC-CRYAB-2
Background
Catalog Number:
CPTC-CRYAB-2
Target Antigen:
Crystallin Alpha B
Isotype:
IgG2a
Species:
Mouse
Last Updated:
08/27/2009
Purchase
- Purchase CPTC-CRYAB-2 (CRYAB-2) - DSHB
Characterization Data [Compare Characterization Data]
Western Blot
Click to enlarge
Western Blot using CPTC-CRYAB-2 as primary Ab against Ag 10408 (lane 2). Also included are molecular wt. standards (lane 1) and mouse IgG control (lane 3).
Characterization SOP Files
Indirect ELISA
Click to enlarge
Indirect ELISA (ie, binding of Antibody to Antigen coated plate)
Characterization SOP Files
Antibody: CPTC-CRYAB-3
Background
Catalog Number:
CPTC-CRYAB-3
Target Antigen:
Crystallin Alpha B
Isotype:
IgG2a
Species:
Mouse
Last Updated:
08/27/2009
Purchase
- Purchase CPTC-CRYAB-3 (CRYAB-3) - DSHB
Characterization Data [Compare Characterization Data]
Western Blot
Click to enlarge
Western Blot using CPTC-CRYAB-3 as primary Ab against Ag 10408 (lane 2). Also included are molecular wt. standards (lane 1) and mouse IgG control (lane 3).
Characterization SOP Files
Indirect ELISA
Click to enlarge
Indirect ELISA (ie, binding of Antibody to Antigen coated plate)
Characterization SOP Files
Antigen: Crystallin Alpha B
Background
NCI Identification Number:
10408
Antigen Name:
Crystallin Alpha B
CPTC Name:
CPTC-CRYAB
Keywords:
CRYAB; Alpha(B)-crystallin; CRYA2; CTPP2; HSPB5; HspB5
Function:
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter
class constitutes the major proteins of vertebrate eye lens and maintains the transparency and
refractive index of the lens. Since lens central fiber cells lose their nuclei during development,
these crystallins are made and then retained throughout life, making them extremely stable
proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and
gamma crystallins are also considered as a superfamily. Alpha and beta families are further
divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. 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 (sHSP also known as the 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. 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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a
missense mutation cosegregated in a family with a desmin-related myopathy.
class constitutes the major proteins of vertebrate eye lens and maintains the transparency and
refractive index of the lens. Since lens central fiber cells lose their nuclei during development,
these crystallins are made and then retained throughout life, making them extremely stable
proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and
gamma crystallins are also considered as a superfamily. Alpha and beta families are further
divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. 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 (sHSP also known as the 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. 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. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a
missense mutation cosegregated in a family with a desmin-related myopathy.
Chromosomal Localization:
11q22.3 - 11q23.1
Expression System:
E. Coli
NCBI Accession Number:
BC007008
Swiss Prot Accession Number:
P02511
DNA Source:
HIP:HsCD00004255
Vector Name:
pMCSG7
Extinction Coefficient:
13980
Buffers:
50mM NH4HC03
Expressed Sequence:
SNAMDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLL
ESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMR
LEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHE
ERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDG
VLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
ESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMR
LEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHE
ERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDG
VLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Native Sequence:
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLES
DLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRL
EKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHE
ERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD
GVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
DLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRL
EKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHE
ERQDEHGFISREFHRKYRIPADVDPLTITSSLSSD
GVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
Calculated Isoelectric Point:
6.75
Molecular Weight:
20431
Last Updated:
01/28/2009
Links
- Uniprot - Uniprot CRYAB
- EnsEMBL - EnsEMBL CRYAB
- Entrez - Entrez CRYAB
Characterization Data
Gel
Click to enlarge
Ag 10408
PAGE of Ag 10408 (with molecular weight standards in lane 1)
Characterization SOP Files
SOPs
Adobe Reader™ required.
Get Adobe Reader for free at Adobe.com
