Analytical Data
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Gene name
FLJ23834
- Application
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Alternative Names
Cadherin-like protein 28; Cadherin-related family member 3; Cdhr3; CDHR3_HUMAN; FLJ43271; Hypothetical protein FLJ23834; Hypothetical protein LOC222256; MGC133292; MGC133293
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6ZTQ4
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Expression Region
776-885aa
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AA Sequence
IFDGEAIDPVTGETYEFNSKTGARKWKDPLTQMPKWKESSHQGAAPRRVTAGEGMGSLRSANWEEDELSGKAWAEDAGLGSRNEGGKLGNPKNRNPAFMNRAYPKPHPGK
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Molecular Weight
37.84 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
FLJ23834 is a recombinant protein that has garnered attention in the field of molecular biology and biomedicine due to its potential roles in cellular processes and its implications in disease mechanisms. Initially identified through large-scale genomic projects, FLJ23834 is thought to be involved in critical cellular functions, including signal transduction and gene regulation. Its expression patterns in various tissues suggest a possible role in development and differentiation, making it a candidate for further study in developmental biology. Moreover, emerging evidence indicates that alterations in the expression of FLJ23834 may be linked to certain pathological conditions, including cancer and autoimmune diseases, which highlights the importance of understanding its biological functions and mechanisms. Researchers are particularly interested in elucidating the structure-function relationship of FLJ23834 to explore its potential as a therapeutic target or biomarker. Advances in recombinant DNA technology have facilitated the production of this protein for experimental purposes, enabling detailed investigations into its biochemical properties and interactions with other molecules. Continued research on FLJ23834 could provide insights not only into its role in normal physiology but also into its potential implications in various diseases, ultimately contributing to the development of novel diagnostic and therapeutic approaches.
