CRYBA2 Rabbit pAb(bs-14071R)-50ul/100ul/200ul

CRYBA2 Rabbit pAb(bs-14071R)-5

0ul/100ul/200ul
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  • ¥1180 - 2800
  • Bioss已认证
  • bs-14071R
  • 2025年10月17日
  • 产品信息以Bioss网站为准
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      50ul/100ul/200ul

    规格:50ul产品价格:¥1180.0
    规格:100ul产品价格:¥1980.0
    规格:200ul产品价格:¥2800.0
    产品编号bs-14071R
    英文名称CRYBA2 Rabbit pAb
    中文名称β晶体体蛋白A2抗体
    英文别名beta A2 crystallin; beta crystallin A2; CRBA2_HUMAN;
    中文别名βA2-crystallin; βA2 crystallin; β crystallin A2.
    产品应用IHC-P=1:100-500, IHC-F=1:100-500, ICC/IF=1:100-500, IF=1:100-500, ELISA=1:5000-10000

    Not yet tested in other applications.
    Optimal working dilutions must be determined by the end user.

    交叉反应 (Human, Mouse, Rat, Dog, Pig, Cow, Horse)
    抗体来源Rabbit
    免疫原KLH conjugated synthetic peptide derived from human CRYBA2
    亚型IgG
    性状Liquid
    纯化方法affinity purified by Protein A
    克隆类型Polyclonal
    理论分子量22 kDa
    浓度1mg/ml
    储存液0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
    亚基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).
    相似性Belongs to the beta/gamma-crystallin family.
    Contains 4 beta/gamma crystallin 'Greek key' domains.
    功能crystallin, beta A2: Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported.
    保存条件Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported. [provided by RefSeq, Jul 2008]

     

    应用推荐稀释比例
    {IHC-P}{1:100-500}
    {IHC-F}{1:100-500}
    {ICC/IF}{1:100-500}
    {IF}{1:100-500}
    {ELISA}{1:5000-10000}

     

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