Tropomodulin-1 (TMOD1) Antibody

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292.5€ (80 µl)

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935106861
info@markelab.com
name
Tropomodulin-1 (TMOD1) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx028742
tested applications
ELISA, WB

Description

TMOD1 is a member of the tropomodulin family. The encoded protein is an actin-capping protein that regulates tropomyosin by binding to its N-terminus, inhibiting depolymerization and elongation of the pointed end of actin filaments and thereby influencing the structure of the erythrocyte membrane skeleton. Multiple transcript variants encoding the same protein have been found for this gene.

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Target: Tropomodulin-1 (TMOD1)
Immunogen: KLH-conjugated synthetic peptide between 170-198 amino acids from the Central region of human TMOD1.
Host
Rabbit
Reactivity
Human
Recommended Dilution
WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Observed MW
Calculated MW: 40.6 kDa
Purification
Purified through a protein A column, followed by peptide affinity purification.
Size 1
80 µl
Size 2
400 µl
Form
Liquid
Tested Applications
ELISA, WB
Buffer
PBS containing 0.09% 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
P28289
Background
Antibody anti-TMOD1
Status
RUO
Note
THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION.

Descripción

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TMOD1 is a member of the tropomodulin family. The encoded protein is an actin-capping protein that regulates tropomyosin by binding to its N-terminus, inhibiting depolymerization and elongation of the pointed end of actin filaments and thereby influencing the structure of the erythrocyte membrane skeleton. Multiple transcript variants encoding the same protein have been found for this gene.

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