Analytical Data
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Gene name
OPCML
- Application
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Alternative Names
OPCML；IGLON1；OBCAM；Opioid-binding Protein/cell adhesion molecule
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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
Q14982-1
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Expression Region
1-322aa
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AA Sequence
MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID DRVTRVAWLN RSTILYAGND KWSIDPRVII LVNTPTQYSI MIQNVDVYDE GPYTCSVQTD NHPKTSRVHL IVQVPPQIMN ISSDITVNEG SSVTLLCLAI GRPEPTVTWR HLSVKEGQGF VSEDEYLEIS DIKRDQSGEY ECSALNDVAA PDVRKVKITV NYPPYISKAK NTGVSVGQKG ILSCEASAVP MAEFQWFKEE TRLATGLDGM RIENKGRMST LTFFNVSEKD YGNYTCVATN KLGNTNASIT LYGPGAVIDG VN
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Molecular Weight
34 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
OPCML (Oligomeric Protein of the Chimeric Membrane-linked protein family) is a glycosylphosphatidylinositol-anchored protein that plays a crucial role in various cellular processes, including cell adhesion, signaling, and differentiation. Research into OPCML has gained prominence due to its potential implications in cancer biology, particularly in the context of tumor development and progression. Studies have shown that OPCML is downregulated in various cancers, suggesting it may function as a tumor suppressor. The understanding of OPCML's structure-function relationship is essential for elucidating its role in tumor biology and developing potential therapeutic strategies. Recombinant OPCML protein has been developed to facilitate functional studies, enabling researchers to investigate its interactions with other cellular molecules and pathways. By producing and characterizing this protein, scientists aim to uncover the biochemical mechanisms by which OPCML influences cancer progression and to explore its potential as a biomarker or therapeutic target in oncology. The ongoing research on OPCML not only sheds light on its biological significance but also opens avenues for innovative approaches in cancer treatment and diagnosis.
