CRYBB2 Antibody - #DF7406
(6)
| Product: | CRYBB2 Antibody |
| Catalog: | DF7406 |
| Description: | Rabbit polyclonal antibody to CRYBB2 |
| Application: | WB IHC |
| Reactivity: | Human, Mouse, Rat |
| Prediction: | Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus |
| Mol.Wt.: | 23kDa; 23kD(Calculated). |
| Uniprot: | P43320 |
| RRID: | AB_2839344 |
Related Downloads
Protocols
Product Info
Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*The optimal dilutions should be determined by the end user.
*Tips:
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Zebrafish(82%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(83%), Xenopus(83%)
Clonality:
Polyclonal
Specificity:
CRYBB2 Antibody detects endogenous levels of total CRYBB2.
RRID:
AB_2839344
Cite Format: Affinity Biosciences Cat# DF7406, RRID:AB_2839344.
Cite Format: Affinity Biosciences Cat# DF7406, RRID:AB_2839344.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Immunogens
Immunogen:
Uniprot:
Gene(ID):
Description:
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. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.
Sequence:
- P43320 CRBB2_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MASDHQTQAGKPQSLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSN
Predictions
Predictions:
Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.
Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Rabbit
100
Xenopus
83
Chicken
83
Zebrafish
82
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence
High(score>80) Medium(80>score>50) Low(score<50) No confidence
PTMs - P43320 As Substrate
| Site | PTM Type | Enzyme | Source |
|---|---|---|---|
| A2 | Acetylation | Uniprot | |
| K42 | Methylation | Uniprot | |
| K68 | Methylation | Uniprot | |
| K76 | Acetylation | Uniprot | |
| T91 | Phosphorylation | Uniprot | |
| S93 | Phosphorylation | Uniprot | |
| S95 | Phosphorylation | Uniprot | |
| S96 | Phosphorylation | Uniprot | |
| S104 | Phosphorylation | Uniprot | |
| T118 | Phosphorylation | Uniprot | |
| K121 | Acetylation | Uniprot | |
| K121 | Methylation | Uniprot | |
| S204 | Phosphorylation | Uniprot |
Research Backgrounds
Function:
Crystallins are the dominant structural components of the vertebrate eye lens.
Subunit Structure:
Homo/heterodimer, or complexes of higher-order. The structure of beta-crystallin oligomers seems to be stabilized through interactions between the N-terminal arms (By similarity).
Family&Domains:
Has a two-domain beta-structure, folded into four very similar Greek key motifs.
Belongs to the beta/gamma-crystallin family.
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