Transmembrane Emp24 Domain-Containing Protein 2 (TMED2) Antibody (HRP)

Este producto es parte de TMED - Transmembrane emp24 domain-containing
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169€ (20 µg)

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935106861
info@markelab.com
name
Transmembrane Emp24 Domain-Containing Protein 2 (TMED2) Antibody (HRP)
category
Primary Antibodies
provider
Abbexa
reference
abx306350
tested applications
ELISA

Description

TMED2 Antibody (HRP) is a Rabbit Polyclonal against TMED2 conjugated to HRP.

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Primary Antibodies
Immunogen Target
Transmembrane Emp24 Domain-Containing Protein 2 (TMED2)
Host
Rabbit
Reactivity
Human
Recommended Dilution
Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
HRP
Isotype
IgG
Purity
> 95%
Purification
Purified by Protein G.
Size 1
20 µg
Size 2
50 µg
Size 3
100 µg
Size 4
200 µg
Size 5
1 mg
Form
Liquid
Tested Applications
ELISA
Buffer
0.01 M PBS, pH 7.4, 0.03% Proclin-300 and 50% Glycerol.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid exposure to light. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q15363
Gene ID
10959
Alias
TMED2, RNP24,p24 family protein beta-1,p24beta1
Background
Antibody anti-TMED2
Status
RUO

Descripción

TMED2, a member of the p24 family, functions as a cargo receptor and vesicle trafficking regulator in the early secretory pathway, mediating protein transport between the ER, ER-Golgi intermediate compartment (ERGIC), and Golgi apparatus. It is a key component of the COPII vesicle coat complex, where it assists in the selective packaging and transport of secretory and membrane proteins. TMED2 also regulates the recycling of vesicles back to the ER through interactions with the COPI coat complex, ensuring efficient cargo flow and ER-Golgi communication. It is highly expressed in tissues with active protein secretion and participates in processes such as receptor trafficking, organelle integrity, and cellular homeostasis. Dysregulation of TMED2 has been implicated in developmental defects, metabolic diseases, and cancers, where altered protein sorting disrupts cellular signaling and growth. Knockdown studies show impaired vesicle transport, disrupted Golgi architecture, and ER stress, highlighting its critical role in maintaining vesicular trafficking, protein quality control, and cellular function.

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