Analytical Data
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Gene name
rpmI
- Application
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Alternative Names
rpmI；Immunoglobulin kappa variable 2-30
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Species
E.coli
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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
P0A7Q1
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Expression Region
7-64aa
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AA Sequence
VRGAAKRFKKTGKGGFKHKHANLRHILTKKATKRKRHLRPKAMVSKGDLGLVIACLPY
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Molecular Weight
33.5 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
Recombinant proteins, particularly those derived from the RPMI (Roswell Park Memorial Institute) cell line, play a pivotal role in biomedical research and therapeutic applications. The RPMI-8226 cell line, established from human multiple myeloma cells, has become a crucial model for studying various aspects of cancer biology, immune responses, and the tumor microenvironment. These cells are often used in the production of recombinant proteins, allowing researchers to explore the complex interactions between proteins involved in cell signaling, apoptosis, and antigen presentation. Furthermore, the use of RPMI-derived recombinant proteins facilitates the development of novel diagnostic tools and therapeutic strategies for treating multiple myeloma and other related malignancies. The ongoing research focuses on optimizing protein expression systems, improving purification techniques, and enhancing the functional characterization of these proteins to better understand their roles in disease progression and therapy resistance. As such, the study of RPMI-derived recombinant proteins remains a significant area of investigation in the quest for innovative treatments and improved patient outcomes in oncology.
