Analytical Data
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Gene name
GULP1
- Application
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Alternative Names
GULP1;CED6;GULP;PTB domain-containing engulfment adapter Protein 1
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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
Q9UBP9
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Expression Region
1-304aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNRAFSR KKDKTWMHTP EALSKHFIPY NAKFLGSTEV EQPKGTEVVR DAVRKLKFAR HIKKSEGQKI PKVELQISIY GVKILEPKTK EVQHNCQLHR ISFCADDKTD KRIFTFICKD SESNKHLCYV FDSEKCAEEI TLTIGQAFDL AYRKFLESGG KDVETRKQIA GLQKRIQDLE TENMELKNKV QDLENQLRIT QVSAPPAGSM TPKSPSTDIF DMIPFSPISH QSSMPTRNGT QPPPVPSRST EIKRDLFGAE PFDPFNCGAA DFPPDIQSKL DEMQEGFKMG LTLEGTVFCL DPLDSRC
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Molecular Weight
37 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
GULP1, a member of the GULP family of proteins, has garnered significant interest due to its roles in cellular processes such as endocytosis, apoptosis, and the regulation of signaling pathways. It primarily functions as an adaptor protein that links ubiquitinated membrane proteins to the clathrin-mediated endocytic machinery, thereby facilitating the internalization and degradation of these proteins. Recent studies have shown that GULP1 is implicated in various physiological and pathological conditions, including cancer progression and neurodegenerative diseases. Its ability to interact with multiple proteins and influence cellular signaling pathways highlights its potential as a therapeutic target. Due to the complexity and specificity of its interactions, the study of recombinant GULP1 proteins has become essential for understanding their functional roles in cellular contexts. Researchers are increasingly focusing on characterizing the structure-function relationships of GULP1 and exploring its potential applications in targeted therapies, making it a crucial area of investigation in contemporary biomedical research. Understanding the precise mechanisms by which GULP1 operates will provide deeper insights into its contributions to cellular homeostasis and disease pathology.











