Thyroid Receptor-Interacting Protein 6 (TRIP6) Antibody

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383.5€ (100 µl)

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935106861
info@markelab.com
name
Thyroid Receptor-Interacting Protein 6 (TRIP6) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx012184
tested applications
ELISA, WB, FCM

Description

This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Thyroid Receptor-Interacting Protein 6 (TRIP6)
Host
Mouse
Reactivity
Human
Recommended Dilution
ELISA: Propose dilution 1/10000, WB: 1/500 - 1/2000, FCM: 1/200 - 1/400. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Monoclonal
Conjugation
Unconjugated
Isotype
IgG1
Purification
Purified from ascites by Protein G chromatography.
Size 1
100 µl
Form
Liquid
Tested Applications
ELISA, WB, FCM
Buffer
PBS, containing 0.05% sodium azide.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q15654
Gene ID
7205
OMIM
602933
Background
Antibody anti-TRIP6
Status
RUO
Note
Concentration: 1 mg/ml - 

Descripción

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This gene is a member of the zyxin family and encodes a protein with three LIM zinc-binding domains. This protein localizes to focal adhesion sites and along actin stress fibers. Recruitment of this protein to the plasma membrane occurs in a lysophosphatidic acid (LPA)-dependent manner and it regulates LPA-induced cell migration. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.

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