Analytical Data
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Gene name
CRIP2
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简介
The CRIP2 protein, also known as cysteine-rich intestinal protein 2, is a protein involved in a variety of cellular processes. CRIP2 protein interacts with TGFB1I1. CRIP2 Protein, Human (sf9) is the recombinant human-derived CRIP2 protein, expressed by Sf9 insect cells , with tag free.
- Application
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Alternative Names
Cysteine-rich protein 2; CRP-2; Protein ESP1
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P52943
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Expression Region
M1-P208
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Protein Length
Full Length
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Molecular Weight
26 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
Related Products
Protein Description
CRIP2 (Cysteine-Rich Protein 2) is a member of the CRIP family of proteins, which are known to play significant roles in cellular processes, including cell growth, differentiation, and response to environmental stresses. Research into CRIP2 has gained traction due to its potential implications in various physiological and pathological contexts, particularly in the development of cardiac and skeletal muscle tissues. Given that CRIP2 contains multiple cysteine-rich motifs, its interactions with metal ions and potential involvement in redox regulation have drawn attention. Studies have suggested that CRIP2 may be implicated in the modulation of signaling pathways linked to oxidative stress and apoptosis, making it a candidate for investigation in diseases such as cancer and heart failure. As a recombinant protein, CRIP2 can be expressed and purified for in vitro studies, enabling researchers to elucidate its biochemical properties, functional roles, and interactions with other proteins. Understanding CRIP2's structure-function relationship is crucial for determining its exact contributions to cellular mechanisms and its potential as a therapeutic target. Thus, the study of CRIP2 not only enhances our comprehension of basic biological functions but may also lead to advancements in disease treatment and the development of novel biomolecular applications.
