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AB132349

Recombinant Human Twist protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human Twist protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 202 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

BHLHA38, TWIST, TWIST1, Twist-related protein 1, Class A basic helix-loop-helix protein 38, H-twist, bHLHa38

1 Images
SDS-PAGE - Recombinant Human Twist protein (GST tag N-Terminus) (AB132349)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Twist protein (GST tag N-Terminus) (AB132349)

12.5% SDS-PAGE analysis of ab132349 stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

WB, ELISA, SDS-PAGE

applications

Biologically active

No

Accession

Q15672

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MMQDVSSSPVSPADDSLSNSEEEPDRQQPPSGKRGGRKRRSSRRSAGGGAGPGGAAGGGVGGGDEPGSPAQGKRGKKSAGCGGGGGAGGGGGSSSGGGSPQSYEELQTQRVMANVRERQRTQSLNEAFAALRKIIPTLPSDKLSKIQTLKLAARYIDFLYQVLQSDELDSKMASCSYVAHERLSYAFSVWRMEGAWSMSASH","proteinLength":"Full Length","predictedMolecularWeight":"47.85 kDa","actualMolecularWeight":null,"aminoAcidEnd":202,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q15672","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The Twist protein also known as Twist1 is a basic helix-loop-helix (bHLH) transcription factor. It has a molecular mass of approximately 21 kDa. Twist is widely expressed in mesodermal tissues during embryonic development including the somites and limb buds. In adults its expression continues in areas involved in tissue regeneration and wound healing.
Biological function summary

Twist plays significant roles in embryogenesis and in wound healing processes. It functions as an important regulator of mesenchymal cell differentiation and is part of the bHLH family of transcription factors which often form dimers to bind specific DNA sequences. Twist modulates the transcription of genes involved in cell movement and survival. It acts as an important player in the epithelial-mesenchymal transition (EMT) a process important for development and cellular dynamics.

Pathways

Twist integrates into multiple biological networks including the Wnt and Notch signaling pathways. It interacts with proteins like β-catenin in the Wnt pathway and Notch receptors impacting cellular proliferation and fate determination. These interactions highlight its role in regulating cellular behavior and influence various processes such as stem cell maintenance and differentiation.

Twist is implicated in cancer and fibrosis. Its overexpression is often observed in aggressive tumors influencing metastasis through its role in EMT. Twist can interact with oncogenic proteins such as MYC in cancer pathways. In fibrosis aberrant Twist activity leads to excessive tissue remodeling and accumulation of connective tissue. Understanding Twist's function and interactions can aid in developing therapeutic strategies targeting these conditions.

Specifications

Form

Liquid

General info

Function

Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of pro-inflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator : NPAS2-BMAL1 heterodimer (By similarity).

Subcellular localisation

Nucleus

Product protocols

Target data

Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of pro-inflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator : NPAS2-BMAL1 heterodimer (By similarity).
See full target information TWIST1

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

The Journal of biological chemistry 294:5082-5093 PubMed30733340

2019

Protein kinase Cα-mediated phosphorylation of Twist1 at Ser-144 prevents Twist1 ubiquitination and stabilizes it.

Applications

Unspecified application

Species

Unspecified reactive species

Roslyn Tedja,Cai M Roberts,Ayesha B Alvero,Carlos Cardenas,Yang Yang-Hartwich,Sydney Spadinger,Mary Pitruzzello,Gang Yin,Carlotta A Glackin,Gil Mor
View all publications

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