Analytical Data
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Gene name
SIAL2
- Application
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Alternative Names
SIAL2；
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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
Q9Y3R4
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Expression Region
1-380aa
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AA Sequence
MASLPVLQKE SVFQSGAHAY RIPALLYLPG QQSLLAFAEQ RASKKDEHAE LIVLRRGDYD APTHQVQWQA QEVVAQARLD GHRSMNPCPL YDAQTGTLFL FFIAIPGQVT EQQQLQTRAN VTRLCQVTST DHGRTWSSPR DLTDAAIGPA YREWSTFAVG PGHCLQLHDR ARSLVVPAYA YRKLHPIQRP IPSAFCFLSH DHGRTWARGH FVAQDTLECQ VAEVETGEQR VVTLNARSHL RARVQAQSTN DGLDFQESQL VKKLVEPPPQ GCQGSVISFP SPRSGPGSPA QWLLYTHPTH SWQRADLGAY LNPRPPAPEA WSEPVLLAKG SCAYSDLQSM GTGPDGSPLF GCLYEANDYE EIVFLMFTLK QAFPAEYLPQ
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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
SIAL2, or sialic acid-binding immunoglobulin-like lectin 2, is a type of protein that plays a crucial role in immune responses and cell signaling. Research into SIAL2 has gained prominence due to its implications in various physiological and pathological processes, including tumor progression and immune evasion. As a member of the siglec (sialic acid-binding immunoglobulin-like lectin) family, SIAL2 interacts with sialylated glycoproteins and glycolipids, influencing cellular communication and adhesion. Understanding SIAL2's structure and function can shed light on its potential as a therapeutic target, particularly in cancer and autoimmune diseases. The exploration of recombinant SIAL2 proteins has been driven by the need to develop specific antibodies or inhibitors that can modulate its activity. Advances in recombinant DNA technology have enabled researchers to produce large quantities of SIAL2 for biochemical studies and potential clinical applications. By elucidating the molecular mechanisms by which SIAL2 operates, scientists aim to develop novel strategies for manipulating immune responses, thus paving the way for innovative treatments in oncology and immunotherapy. The ongoing research on SIAL2 not only highlights its importance in basic biology but also its potential utility in translational medicine. As such, SIAL2 serves as a promising avenue for future studies aimed at improving our understanding of immune regulation and developing targeted therapeutics.
