Analytical Data
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Gene name
Gremlin-1
- Application
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Alternative Names
Cysteine knot superfamily 1, BMP antagonist 1 Down-regulated in Mos-transformed cells protein
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Species
Rat
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O35793
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Expression Region
25-184aa
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Molecular Weight
34.2 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
Related Products
Protein Description
Gremlin-1, a member of the Dan family of extracellular matrix proteins, has emerged as a significant focus of research due to its role in embryonic development and tissue homeostasis. Originally identified as an antagonist of bone morphogenetic proteins (BMPs), Gremlin-1 has been implicated in various physiological processes, including cell proliferation, differentiation, and apoptosis. Abnormal expression of Gremlin-1 has been associated with several pathological conditions, such as cancer, fibrosis, and congenital malformations. As a result, understanding the molecular mechanisms underlying Gremlin-1 function has become crucial for developing therapeutic strategies aimed at modulating its activity. Recent studies have highlighted its involvement in various signaling pathways and raised interest in its potential as a biomarker for disease progression and a target for intervention. The production of recombinant Gremlin-1 proteins has enabled more detailed functional analyses and the exploration of its interactions with other signaling molecules, further elucidating its biological roles. This research is paving the way for novel approaches in regenerative medicine and the treatment of diseases where Gremlin-1 plays a pivotal role.
