Analytical Data
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Gene name
LN
- Application
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Alternative Names
LN;CSDD2;Protein lin-28 homolog B
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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
Q6ZN17
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Expression Region
1-250aa
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AA Sequence
MAEGGASKGG GEEPGKLPEP AEEESQVLRG TGHCKWFNVR MGFGFISMIN REGSPLDIPV DVFVHQSKLF MEGFRSLKEG EPVEFTFKKS SKGLESIRVT GPGGSPCLGS ERRPKGKTLQ KRKPKGDRCY NCGGLDHHAK ECSLPPQPKK CHYCQSIMHM VANCPHKNVA QPPASSQGRQ EAESQPCTST LPREVGGGHG CTSPPFPQEA RAEISERSGR SPQEASSTKS SIAPEEQSKK GPSVQKRKKT
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Molecular Weight
27 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
LN (Laminin) recombinant proteins are essential tools in cell biology and tissue engineering due to their crucial role in cellular adhesion, differentiation, and tissue development. Laminins are a family of glycoproteins found in the extracellular matrix (ECM), playing a pivotal role in the architecture of tissues and influencing cell behavior via their interactions with cell-surface receptors. The study of LN recombinant proteins allows researchers to better understand these interactions and the biology of various cell types, including stem cells. With advances in genetic engineering, recombinant techniques enable the production of specific laminin isoforms, facilitating the investigation of their unique functions in various biological processes, such as wound healing, cancer metastasis, and neural development. Moreover, the application of LN recombinant proteins in biomaterials has shown promising results in enhancing cell adhesion and promoting tissue regeneration. Consequently, ongoing research in this area aims to optimize the use of LN recombinant proteins for therapeutic applications, such as developing scaffolds for regenerative medicine or improving the efficacy of drug delivery systems, thereby advancing our understanding of ECM dynamics and its potential in clinical therapies.











