ABN185
Anti-alpha B-crystallin Antibody
from rabbit, purified by affinity chromatography
Synonyma:
Alpha-crystallin B chain, Alpha(B)-crystallin, Heat shock protein beta-5, Renal carcinoma antigen NY-REN-27, Rosenthal fiber component
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Doporučené produkty
biological source
rabbit
Quality Level
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
purified by
affinity chromatography
species reactivity
bovine, human, rat
species reactivity (predicted by homology)
horse (based on 100% sequence homology), rhesus macaque (based on 100% sequence homology), ox (based on 100% sequence homology), mouse (based on 100% sequence homology)
technique(s)
immunohistochemistry: suitable (paraffin)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
bovine ... Cryab(281719)
human ... CRYAB(1410)
mouse ... Cryab(12955)
rat ... Cryab(25420)
General description
Alpha B-crystallin is a major structural protein in the vertebrate eye lens, but is also found in cardiac and skeletal muscles, kidney, and brain. Alpha B-crystallin is also found to be a component of Rosenthal fibers and a consistent tissue marker of epileptic foci. It occurs as large aggregates of up to 106 Da, composed of two proteins, αA- and αB-crystallin. The αA gene encodes a polypeptide of 173 residues, while αB-crystallin gene encodes a 175 residue polypeptide. αB-crystallin, like the small heat shock proteins (sHsp′s), is induced by heat or osmotic shock and is upregulated by stress. α-crystallin and the sHsp′s protect other proteins from heat-induced aggregation. The two other crystallin families, β and ɣ, are homologous to each other but not to the α-family or the sHsp′s.
Specificity
This antibody recognizes the N-terminus of alpha B-crystallin.
Immunogen
Epitope: N-terminus
KLH-conjugated linear peptide corresponding to the N-terminus human alpha B-crystallin.
Application
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected Alpha-crystallin B chain in rat lens fiber tissue. A 1:2,000 dilution from a representative lot detected Alpha-crystallin B chain in strong rat lens fiber tissue (data not provided). A 1:1,000 dilution from a representative lot detected Alpha-crystallin B chain in strong muscle fiber tissue (data also not provided). It is recommended to use a 1:2,000 dilution only for strong rat lens fiber tissue.
Western Blot analysis: 0.05 µg/mL of this antibody detected Alpha-crystallin B chain in 10 µg of human kidney and calf kidney tissue lysate.
Western Blot analysis: 0.05 µg/mL of this antibody detected Alpha-crystallin B chain in 10 µg of human kidney and calf kidney tissue lysate.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Developmental Neuroscience
Developmental Neuroscience
This Anti-alpha B-crystallin Antibody is validated for use in WB, IH(P) for the detection of alpha B-crystallin.
Quality
Evaluted by Western Blot in bovine calf lens tissue lysate.
Western Blot analysis: 0.05 µg/mL of this antibody detected Alpha-crystallin B chain in 10 µg of bovine calf lens tissue lysate.
Western Blot analysis: 0.05 µg/mL of this antibody detected Alpha-crystallin B chain in 10 µg of bovine calf lens tissue lysate.
Target description
~20 kDa observed. Uncharacterized bands at ~37 and 43 kDa may be observed in some cell lyates.
Physical form
Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Analysis Note
Control
Bovine calf lens, human kidney and calf kidney tissue lysate
Bovine calf lens, human kidney and calf kidney tissue lysate
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Osvědčení o analýze (COA)
Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.
Již tento produkt vlastníte?
Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.
Fermin Moreno et al.
PloS one, 12(6), e0178093-e0178093 (2017-06-09)
The co-occurrence of the c.709-1G>A GRN mutation and the p.A152T MAPT variant has been identified in 18 Basque families affected by frontotemporal dementia (FTD). We aimed to investigate the influence of the p.A152T MAPT variant on the clinical and neuropathological
Sandip K Nandi et al.
Glycoconjugate journal, 38(3), 347-359 (2020-11-28)
Proteins in the eye lens have negligible turnover and therefore progressively accumulate chemical modifications during aging. Carbonyls and oxidative stresses, which are intricately linked to one another, predominantly drive such modifications. Oxidative stress leads to the loss of glutathione (GSH)
AAV2-Mediated Expression of HspB1 in RGCs Prevents Somal Damage and Axonal Transport Deficits in a Mouse Model of Ocular Hypertension.
Nam, et al.
Translational vision science & technology, 11, 8-8 (2022)
Sandip K Nandi et al.
Experimental eye research, 182, 1-9 (2019-03-09)
Acetylation of lysine residues occurs in lens proteins. Previous studies have shown an improvement in the chaperone activity of αA-crystallin upon acetylation. Sirtuins are NAD+-dependent enzymes that can deacylate proteins. The roles of sirtuins in regulating the acetylation of lens
Sandip K Nandi et al.
The Journal of biological chemistry, 295(17), 5701-5716 (2020-03-19)
Lens proteins become increasingly cross-linked through nondisulfide linkages during aging and cataract formation. One mechanism that has been implicated in this cross-linking is glycation through formation of advanced glycation end products (AGEs). Here, we found an age-associated increase in stiffness
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