Analytical Data
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Gene name
CNR1
- Application
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Alternative Names
CNR1；CNR；Cannabinoid receptor 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
P21554
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Expression Region
1-472aa
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AA Sequence
MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNPQLVPADQVNITEFYNKSLSSFKENEENIQCGENFMDIECFMVLNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFIDFHVFHRKDSRNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCEKLQSVCSDIFPHIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNAASVHRAAESCIKSTVKIAKVTMSVSTDTSAEAL
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Molecular Weight
54.6 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
Survivin, a member of the inhibitor of apoptosis protein (IAP) family, has emerged as a crucial player in cancer biology due to its dual role in inhibiting apoptosis and regulating cell division. First identified as a key factor in the regulation of the mitotic spindle during cell division, Surv protein is notably overexpressed in a variety of tumors while being absent in most normal differentiated tissues, making it an attractive target for therapeutic intervention. Research has revealed that Survivin contributes to tumorigenesis by promoting cell proliferation, inhibiting apoptotic processes, and enhancing tumor cell migration and invasion. Its expression correlates with poor prognosis in several cancers, including breast, prostate, and colorectal cancer. Consequently, the development of recombinant Survivin proteins has gained considerable attention within the scientific community, with aims to understand their functional roles and therapeutic potential. Investigating the structure and function of Surv as a recombinant protein can provide insights into its interactions with other cellular molecules and elucidate the mechanisms underlying its anti-apoptotic and cell cycle regulatory functions. Moreover, these studies may foster the development of innovative cancer treatment strategies, such as survivin-targeted therapies and vaccines, to selectively eliminate cancer cells while sparing normal tissues. As a result, the ongoing research into recombinant Survivin proteins holds promise for advancing our understanding of cancer pathology and improving clinical outcomes for patients suffering from malignancies characterized by dysregulated Survivin expression.
