Analytical Data
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Gene name
VGLL2
- Application
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Alternative Names
VGLL2; VITO1; Transcription cofactor vestigial-like Protein 2; Vgl-2; Protein VITO1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N8G2
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Expression Region
1-317 aa
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AA Sequence
MSCLDVMYQV YGPPQPYFAA AYTPYHQKLA YYSKMQEAQE CNASPSSSGS GSSSFSSQTP ASIKEEEGSP EKERPPEAEY INSRCVLFTY FQGDISSVVD EHFSRALSQP SSYSPSCTSS KAPRSSGPWR DCSFPMSQRS FPASFWNSAY QAPVPPPLGS PLATAHSELP FAAADPYSPA ALHGHLHQGA TEPWHHAHPH HAHPHHPYAL GGALGAQAAP YPRPAAVHEV YAPHFDPRYG PLLMPAASGR PARLATAPAP APGSPPCELS GKGEPAGAAW AGPGGPFASP SGDVAQGLGL SVDSARRYSL CGASLLS
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Molecular Weight
33.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
VGLL2 (vestigial like 2) is a transcriptional co-regulator that plays a crucial role in various biological processes, including cell differentiation, proliferation, and tissue homeostasis. It is known to influence the activity of several transcription factors, particularly in the context of muscle and cardiac development. Researchers have become increasingly interested in VGLL2 due to its implications in various diseases, including cancer and cardiovascular disorders. Studies have shown that VGLL2 can affect tumorigenesis by modulating pathways related to cell growth and apoptosis. The ability of VGLL2 to interact with other proteins and its role in gene expression regulation make it a promising target for therapeutic interventions. Current research often focuses on the recombinant expression of VGLL2 to better understand its structure-function relationships and to explore its potential as a biomarker or therapeutic target. By using recombinant protein techniques, scientists aim to analyze VGLL2's interactions with other proteins and its downstream effects in relevant cellular contexts. This work is essential for elucidating the mechanisms by which VGLL2 contributes to normal physiology and disease states, paving the way for new strategies in disease management.
