Analytical Data
-
Gene name
REG-4
-
简介
REG-4 is a calcium-independent lectin with mannose-binding specificity that retains carbohydrate recognition activity even in acidic environments. Its ability to act independently of calcium indicates its potent and versatile lectin activity. REG-4 Protein, Human (HEK293, Fc) is the recombinant human-derived REG-4 protein, expressed by HEK293 , with N-hFc labeled tag.
- Application
-
Alternative Names
Regenerating islet-derived protein 4; GISP; RELP; REG4
-
Species
Human
-
Source
HEK293
-
Tag
N-hFc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BYZ8-1
-
Expression Region
D23-P158
-
Protein Length
Full Length of Isoform-1 Mature Protein
-
Molecular Weight
45 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
S100A9, a member of the S100 protein family, is a calcium-binding protein that plays a crucial role in various biological processes, including inflammation, cell proliferation, and apoptosis. It is predominantly expressed in myeloid cells and has been identified as a key player in the immune response, particularly in chronic inflammatory diseases, autoimmune disorders, and cancer. Research has shown that S100A9 can form heterodimers with S100A8, enhancing its biological activity and contributing to the formation of pro-inflammatory complexes. The dysregulation of S100A9 expression is associated with several pathological conditions, including rheumatoid arthritis, inflammatory bowel disease, and various types of malignancies. Given its significant role in mediating inflammatory responses, S100A9 has emerged as a potential biomarker for disease diagnosis and prognosis, as well as a target for therapeutic interventions. Recombinant S100A9 protein is essential for studying its structure-function relationships, understanding its interactions with other proteins, and exploring its mechanism of action in inflammatory pathways. The production and characterization of S100A9 recombinant protein have garnered attention for their implications in developing novel therapeutic strategies aimed at modulating inflammation and improving outcomes in related diseases. Thus, the investigation of S100A9 recombinant protein serves as a critical avenue in biomedicine, offering insights into its role as a potential therapeutic target and advancing our understanding of inflammatory mechanisms.
