Crystallin, beta B1 Proteine (CRYBB1)

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Zusätzlich bieten wir Ihnen Crystallin, beta B1 Antikörper (27) und Crystallin, beta B1 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
CRYBB1 1414 P53674
CRYBB1 12960 Q9WVJ5
CRYBB1 25421 P02523
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Showing 10 out of 19 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 26 bis 31 Tage
4.115,41 €
Details
Insektenzellen Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 46 Days
5.173,33 €
Details
HOST_Escherichia coli (E. coli) Human His tag 100 μg Anmelden zum Anzeigen 11 bis 15 Tage
272,38 €
Details
HOST_Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 7 bis 8 Tage
345,60 €
Details
HOST_HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen 6 bis 8 Tage
748,00 €
Details
Hefe Huhn His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.479,36 €
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Hefe Wildschwein His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.509,05 €
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Hefe Ratte His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.512,54 €
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Hefe Rind (Kuh) His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.521,27 €
Details
HOST_Escherichia coli (E. coli) Ratte His tag   100 μg Anmelden zum Anzeigen 13 bis 17 Tage
518,10 €
Details

CRYBB1 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,
, ,
Mouse (Murine) ,
,
Rat (Rattus) ,

Am meisten referenzierte Crystallin, beta B1 Proteine

  1. Human CRYBB1 Protein expressed in Escherichia coli (E. coli) - ABIN667015 : Annunziata, Pande, Pande, Ogun, Lubsen, Benedek: Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-crystallin. in Biochemistry 2005 (PubMed)
    Zeige alle 2 Referenzen für 667015

Weitere Proteine zu Crystallin, beta B1 (CRYBB1) Interaktionspartnern

Zebrafish Crystallin, beta B1 (CRYBB1) Interaktionspartner

  1. fundamental transcriptional regulatory mechanism of the betaB1-crystallin gene has been well conserved between humans and zebrafish

Xenopus laevis Crystallin, beta B1 (CRYBB1) Interaktionspartner

  1. The ontogeny and localization of the alphaA-crystallin (zeige CRYAA Proteine) and betaB1-crystallin during embryonic lens development and regeneration indicated a different development program, although they have identical origins, the ectoderm.

Human Crystallin, beta B1 (CRYBB1) Interaktionspartner

  1. CRYBB1 partial duplication ad complete duplication of CRYBA4 (zeige CRYbA4 Proteine) identified in a family with autosomal dominant congenital cataract.

  2. Molecular dynamic simulation studies indicated that the mutation decreased the subunit binding energy and modified the distribution of surface electrostatic potentials. More importantly, the mutation separated two interacting loops in the C-terminal domain, which shielded the hydrophobic core from solvent in native betaB1-crystallin.

  3. Congenital microcornea-cataract syndrome-causing mutation X253R increases betaB1-crystallin hydrophobicity to promote aggregate formation

  4. Despite the disruption of betaB1-crystallin assembly, the thermal stability of betaB1-crystallin was increased by the mutation accompanied by the reduction of thermal aggregation at high temperatures

  5. study identified a novel heterozygous p.Ser129Arg mutation in CRYBB1 in a congenital cataract-microcornea syndrome family of Chinese origin

  6. Analyses of 20 Chinese families with hereditary nuclear congenital cataract revealed 3 novel mutations. Two of these mutations (V146M and I21N) affected betaB2-crystallin (CRYBB2 (zeige CRYbB2 Proteine)). One mutation (R233H) was detected in betaB1-crystallin (CRYBB1).

  7. Variant alleles of the CRYBB1 and CRYBB2 (zeige CRYbB2 Proteine) genes were found, none are considered pathogenic.

  8. Mutation G220X is associated with autosomal dominant cataract.

  9. fundamental transcriptional regulatory mechanism of the betaB1-crystallin gene has been well conserved between humans and zebrafish

  10. the sequence of betaB2-crystallin (zeige CRYbB2 Proteine) appears well optimized for domain swapping

Mouse (Murine) Crystallin, beta B1 (CRYBB1) Interaktionspartner

  1. Removal of the N-terminal extension of beta B1-crystallin has major effects on the physical properties of the protein by increasing the self-association potential and by blocking heteromolecular associations with beta A3-crystallin (zeige CRYBA1 Proteine).

Pig (Porcine) Crystallin, beta B1 (CRYBB1) Interaktionspartner

  1. Tissue expression analysis indicated that that swine SDHB (zeige SDHB Proteine), SNRPA (zeige SNRPA Proteine) and CRYBB1 genes were differentially expressed in tissues including fat, lung, muscle, small intestine, kidney, large intestine, spleen and liver.

Crystallin, beta B1 (CRYBB1) Protein Überblick

Protein Überblick

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, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3.

Genbezeichner und Symbole assoziert mit Crystallin, beta B1 Proteine (CRYBB1)

  • crystallin, beta B1 (crybb1)
  • crystallin, beta B1 (CRYBB1)
  • crystallin, beta B1 (Crybb1)
  • 3110006K12Rik Protein
  • BB1CRY Protein
  • CATCN3 Protein
  • CRYB1 Protein
  • CRYB11 Protein
  • Crybb1 Protein
  • CTRCT17 Protein
  • zgc:92706 Protein

Bezeichner auf Proteinebene für Crystallin, beta B1 Proteine (CRYBB1)

crystallin, beta B1 , crystallin B1 , beta B1 crystallin , betaB1-crystallin , beta-B1 crystallin , beta-crystallin B1 , eye lens structural protein , beta-35 , beta crystallin subunit beta B1

GENE ID SPEZIES
114418 Danio rerio
397730 Xenopus laevis
458727 Pan troglodytes
486333 Canis lupus familiaris
550022 Xenopus (Silurana) tropicalis
100307054 Cavia porcellus
1414 Homo sapiens
12960 Mus musculus
25421 Rattus norvegicus
282205 Bos taurus
374000 Gallus gallus
780429 Sus scrofa
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