Analytical Data
-
Gene name
VSIG2
- Application
-
Alternative Names
VSIG2;CTH;CTXL;;V-set and immunoglobulin domain-containing Protein 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96IQ7
-
Expression Region
24-243aa
-
AA Sequence
VEVKVPTEPLSTPLGKTAELTCTYSTSVGDSFALEWSFVQPGKPISESHP ILYFTNGHLYPTGSKSKRVSLLQNPPTVGVATLKLTDVHPSDTGTYLCQV NNPPDFYTNGLGLINLTVLVPPSNPLCSQSGQTSVGGSTALRCSSSEGAP KPVYNWVRLGTFPTPSPGSMVQDEVSGQLILTNLSLTSSGTYRCVATNQM GSASCELTLSVTEPSQGRVAVDHHHHHH
-
Molecular Weight
24 kDa
-
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
VSIG2 (V-set and immunoglobulin domain containing 2) is a member of the immunoglobulin superfamily and plays a significant role in immune regulation. It is primarily expressed in immune cells, such as T cells and dendritic cells, and has been implicated in various biological processes, including cell adhesion, signaling, and immune response modulation. Research has shown that VSIG2 is involved in controlling the balance between immune activation and tolerance, making it a crucial factor in autoimmune diseases and cancer immunotherapy. Given its emerging significance in immunology, scientists have increasingly focused on understanding the structure and function of VSIG2, especially in the context of its role as a potential therapeutic target. Recent studies have employed techniques such as gene editing, protein expression, and crystal structure analysis to elucidate the mechanisms by which VSIG2 interacts with other immune components. These investigations aim not only to clarify its function in immune modulation but also to explore its potential applicability in developing novel treatment strategies for immune-related conditions. As the scientific community continues to uncover the intricate roles of immune receptors like VSIG2, a deeper understanding of its structure-function relationship may pave the way for innovative approaches in immunotherapy, ultimately contributing to improved outcomes in autoimmune diseases and cancer. The ongoing research into VSIG2 thus represents a promising avenue for advancing our knowledge of immune regulation and therapeutic interventions.











