Analytical Data
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Gene name
GRP
- Application
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Alternative Names
GRP；Gastrin-releasing peptide
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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
Q3ZCW2
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSHMAGSVADSDAVVKLDDGHLNNSLSSP VQADVYFPRLIVPFCGHIKGGMRPGKKVLVMGIVDLNPESFAISLTCGDS EDPPADVAIELKAVFTDRQLLRNSCISGERGEEQSAIPYFPFIPDQPFRV EILCEHPRFRVFVDGHQLFDFYHRIQTLSAIDTIKINGDLQITKLG
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Molecular Weight
22 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
GRP (Glycoprotein Receptor Protein) recombinant proteins have emerged as a significant focus in biomedical research due to their essential roles in various physiological and pathological processes. These proteins are often involved in cell signaling, molecular recognition, and immune responses, making them critical for the development of novel therapeutic strategies. Recent advancements in genetic engineering and recombinant DNA technology have facilitated the production of GRP proteins in host systems, allowing researchers to investigate their structure-function relationships and biological interactions in greater detail. Notably, the ability to modify these proteins, such as through glycosylation patterns, enhances their functional diversity and potential application in targeted therapies, vaccines, and diagnostic tools. As diseases like cancer, autoimmune disorders, and infectious diseases continue to pose significant health challenges, understanding the mechanisms underlying GRP interactions becomes vital. Ongoing studies aim to unravel the complexities of GRP functions, paving the way for innovative approaches to disease treatment and prevention. The integration of GRP research with emerging technologies like CRISPR and advanced proteomics further underscores its potential impact on the field of medicine.
