Search Thermo Fisher Scientific
Disclaimer
Clicking the images or links will redirect you to a website hosted by BenchSci that provides third-party scientific content. Neither the content nor the BenchSci technology and processes for selection have been evaluated by us; we are providing them as-is and without warranty of any kind, including for use or application of the Thermo Fisher Scientific products presented.
Invitrogen
Catenin alpha-1 Recombinant Rabbit Monoclonal Antibody (SC0619)
高级验证
This Antibody was verified by Knockout to ensure that the antibody binds to the antigen stated.
产品信息
MA5-32216
应用
建议稀释比
已发表文章
产品规格
种属反应
Human,
Mouse,
Rat
宿主/亚型
Rabbit
/ IgG
Expression System
HEK293 cells
分类
Recombinant Monoclonal
类型
Antibody
克隆号
SC0619
抗原
Recombinant protein within Human alpha 1 Catenin aa 1-90
偶联物
形式
Liquid
浓度
1 mg/mL
纯化类型
Protein A
保存液
TBS, pH 7.4, with 40% Glycerol, 0.05% BSA
内含物
0.05% sodium azide
保存条件
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
运输条件
Wet ice
RRID
AB_2809503
产品详细信息
Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
靶标信息
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。
篇参考文献 (0)
您是否在文献中引用过该产品？请点击下方按钮邮件告知我们。
生物信息学
蛋白别名: 102 kDa cadherin-associated protein; alpha E catenin; Alpha E-catenin; alpha(E)-catenin; alpha-E-catenin; cadherin associated protein; Cadherin-associated protein; CAP102; catenin (cadherin associated protein), alpha 1; catenin (cadherin-associated protein), alpha 1, 102kDa; catenin alpha 1; Catenin alpha-1; catenin, alpha 1; Renal carcinoma antigen NY-REN-13
基因别名: 2010010M04Rik; AA517462; AI988031; CAP102; Catna1; CTNNA1; MDPT2
UniProt ID: (Human) P35221, (Mouse) P26231
Entrez Gene ID: (Human) 1495, (Rat) 307505, (Mouse) 12385
ovarian follicle development
actin filament organization
cell adhesion
establishment or maintenance of cell polarity
negative regulation of neuroblast proliferation
aging
male gonad development
gap junction assembly
axon regeneration
adherens junction organization
cellular protein localization
odontogenesis of dentin-containing tooth
apical junction assembly
response to estrogen
positive regulation of smoothened signaling pathway
positive regulation of muscle cell differentiation
protein heterooligomerization
cellular response to indole-3-methanol
epithelial cell-cell adhesion
negative regulation of cell motility
negative regulation of integrin-mediated signaling pathway
negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
positive regulation of extrinsic apoptotic signaling pathway in absence of ligand
response to organic cyclic compound
regulation of cell proliferation
negative regulation of apoptotic process
