Thermo Fisher Scientific Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody
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카탈로그 번호 | CAS 번호 | 설명 | 상태 | 단위 | 판매가 | 할인가 | 가격(VAT포함) | 수량 / 장바구니 / 찜 |
PA5143662 | - | Thermo Fisher Scientific PA5143662 Phospho-Catenin alpha-1 (Tyr148) Polyclonal Antibody 100 ul pk | 재고문의 | pk | 789,000원 | - | 867,900원 |
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Applications
Tested Dilution
Publications
Western Blot (WB)
1:100
Product Specifications
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. This peptide sequence is highly conserved in rat and mouse alpha1-Catenin, but is not conserved in alpha2-Catenin or alpha3-Catenin.
Conjugate
Unconjugated Unconjugated Unconjugated
Form
Liquid
Concentration
0.5 mg/mL
Purification
Antigen affinity chromatography
Storage buffer
PBS with 1mg/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). The antibody 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
Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherence junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play 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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