Analytical Data
-
Gene name
LXN
- Application
-
Alternative Names
LXN;Latexin
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BS40
-
Expression Region
1-222aa
-
AA Sequence
MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYHLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFT FEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDY TILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
LXN, or leucine zipper nucleoprotein, is a crucial protein implicated in various cellular processes, including cell proliferation, apoptosis, and differentiation. Recent studies have highlighted its role in the regulation of gene expression, particularly in the context of cancer and other diseases. The overexpression or dysregulation of LXN has been associated with several types of malignancies, suggesting its potential as a biomarker for tumor progression and a target for therapeutic intervention. The intricate mechanisms by which LXN modulates cell signaling pathways and its interactions with other cellular proteins have driven researchers to explore recombinant LXN protein for both functional studies and therapeutic development. The use of recombinant DNA technology to produce LXN offers a reliable method for obtaining purified protein, enabling the characterization of its biological functions and structural properties. Furthermore, studying LXN in various model systems could elucidate the role of this protein in disease contexts and pave the way for novel treatments. As researchers continue to unravel the multifaceted roles of LXN, there is growing interest in its potential applications in biotechnology and medicine, making it a focal point for ongoing research endeavors.
