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Thermo Fisher Scientific Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody
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Thermo Fisher Scientific Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody

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Phospho-alpha1-Catenin (Tyr148) 폴리클로날 항체로 인간, 마우스, 랫트 반응성. Western blot에 적합하며, 항원 친화 크로마토그래피로 정제됨. 세포 접착 및 액틴 필라멘트 조절 연구에 유용. 연구용으로만 사용 가능.

카탈로그번호
PA5143662
판매단위
pk
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마지막 업데이트 2025. 08. 03. 오전 09:09
Thermo Fisher Scientific PA5143662 Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody 100 ul pk판매 단위 pk ·
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786,900원VAT 포함 865,590원

Thermo Fisher Scientific · Thermo Fisher Scientific Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody

Applications

Western Blot (WB)

  • Tested Dilution: 1:100
  • Publications: [References not provided]

Product Specifications

항목 내용
Species Reactivity Human, Mouse, Rat
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen Phospho-alpha1-Catenin (Tyr-148) synthetic peptide (coupled to KLH), corresponding to amino acid residues around tyrosine 148 in human alpha1-Catenin. Highly conserved in rat and mouse alpha1-Catenin, not conserved in alpha2 or alpha3-Catenin.
Conjugate Unconjugated
Form Liquid
Concentration 0.5 mg/mL
Purification Antigen affinity chromatography
Storage Buffer PBS with 1 mg/mL BSA, 50% glycerol
Contains 0.05% sodium azide
Storage Conditions -20°C, Avoid Freeze/Thaw Cycles
Shipping Conditions Wet ice
RRID AB_2942890

Product Specific Information

This antibody was cross-adsorbed to unrelated phospho-tyrosine peptide before affinity purification using phospho-alpha1-Catenin (Tyr-148) peptide (without carrier). It detects a 102 kDa protein corresponding to the molecular mass of alpha1-Catenin on SDS-PAGE immunoblots of rat PC12 cells treated with pervanadate.


Target Information

Alpha1-Catenin associates with the cytoplasmic domain of various cadherins, forming complexes linked to the actin filament network—critical for cadherin-mediated cell adhesion. It interacts with both E- and N-cadherins. While originally thought to stably link cadherins to actin at adherens junctions, studies show CTNNA1 does not bind F-actin when in complex form, suggesting a dynamic linkage mechanism. The homodimeric form may regulate actin filament assembly and inhibit branching by competing with the Arp2/3 complex, playing a crucial role in cell differentiation.


For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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