Analytical Data
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Gene name
CL-P1/COLEC12
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简介
Collectin-12 is a family of Ca2+-dependent, C-type lectins that contain a collagenous domain and function as recognition molecules for molecular patterns found on pathogens (1 - 4). CL-P1/COLEC12 Protein, Rhesus Macaque (sf9, His) is the recombinant Rhesus Macaque-derived CL-P1/COLEC12 protein, expressed by Sf9 insect cells , with N-His labeled tag.
- Application
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Alternative Names
Collectin-12; Nurse cell scavenger receptor 2; CL-P1; Nsr2
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Species
Rhesus Macaque
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Source
Baculovirus
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
F6RUR9
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Expression Region
A86-L727
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Protein Length
Partial
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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
Related Products
Protein Description
CL-P1, also known as COLEC12, is a C-type lectin receptor that plays a significant role in the innate immune system by recognizing pathogen-associated molecular patterns (PAMPs), which are crucial for the host's defense mechanisms. Research on CL-P1/COLEC12 has gained traction due to its involvement in various biological processes, including the regulation of inflammation, the modulation of immune responses, and the promotion of cellular adherence during pathogen recognition. Notably, COLEC12 has been implicated in the clearance of pathogens, such as bacteria and viruses, suggesting its potential as a therapeutic target in infectious diseases. Moreover, recent studies highlight its role in various pathological conditions, including cancer and autoimmune diseases, where dysregulation of immune responses occurs. The exploration of recombinant forms of CL-P1/COLEC12 facilitates a deeper understanding of its structure-function relationship and biological implications. It opens avenues for developing novel immunotherapeutic strategies that can harness or modulate its activity, leading to potential treatments that enhance disease resistance or mitigate harmful inflammation. Therefore, the study of CL-P1/COLEC12 recombinant proteins is pivotal in unraveling the complexities of immune regulation and holds promise for advancing therapeutic interventions in a range of diseases.
