Analytical Data
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Gene name
CH1
- Application
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Alternative Names
CH1；C1orf9；CH1；OPT；SUN domain-containing ossification factor
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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
P30438
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Expression Region
23-92aa
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AA Sequence
EICPAVKRDVDLFLTGTPDEYVEQVAQYKALPVVLENARILKNCVDAKMTEEDKENALSVLDKIYTSPLC
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Molecular Weight
15.3 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
CH1 recombinant protein, derived from the CH1 domain of antibody light chains, plays a significant role in various biotechnological and therapeutic applications. The CH1 domain is crucial for the stability and functionality of antibodies, which are essential tools in medicine, diagnostics, and research. With the growing need for humanized antibodies in the treatment of diseases such as cancer and autoimmune disorders, the development and production of CH1 recombinant proteins have become increasingly important. These proteins facilitate the engineering of novel antibody formats, improve the yield and stability of antibody production, and enhance the efficacy of therapeutic antibodies. By utilizing recombinant DNA technology, CH1 proteins can be expressed in multiple systems, including bacteria, yeast, and mammalian cells, allowing for scalable production and fine-tuning of their properties. The study of CH1 recombinant proteins also aids in understanding the structure-function relationships within antibodies, enabling the design of more effective biopharmaceuticals. As research in this area continues to evolve, CH1 recombinant proteins are expected to play a pivotal role in advancing antibody therapeutics and improving patient outcomes.
