Analytical Data
-
Gene name
RANTES
- Application
-
Alternative Names
CCL5;D17S136E;SCYA5;C-C motif chemokine 5
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P13501
-
Expression Region
24 -91aa
-
AA Sequence
SPYSSDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS
-
Molecular Weight
10 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
RANTES, or Regulated upon Activation, Normal T Cell Expressed and Secreted, is a crucial chemokine belonging to the C-C chemokine family that plays a significant role in the immune response by attracting immune cells to sites of inflammation. Its production is primarily triggered by activated T cells, monocytes, and other immune cells, making it a key player in various inflammatory conditions and diseases, including autoimmune disorders, infections, and cancer. The interest in RANTES recombinant protein stems from its potential therapeutic applications, particularly in modulating immune responses. Research has focused on the characterization of recombinant RANTES due to its ability to enhance T cell migration and activation, which can be harnessed in vaccine development and immunotherapy. Moreover, manipulating RANTES levels could offer novel strategies for treating diseases characterized by inappropriate inflammatory responses. Advances in biotechnology have facilitated the production of functional RANTES proteins in recombinant systems, allowing for detailed studies into its biochemical properties and interactions with receptors. As a result, understanding the biology and therapeutic potential of RANTES recombinant protein continues to be a significant area of research, with implications for developing new treatments for a range of immunological conditions.
