Analytical Data
-
Gene name
OA
- Application
-
Alternative Names
OA;MER6;Leukocyte surface antigen CD47
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q08722
-
Expression Region
19-139aa
-
AA Sequence
QLLFNKTKSVEFTFCNDTVVIPCFVTNMEAQNTTEVYVKWKFKGRDIYTF DGALNKSTVPTDFSSAKIEVSQLLKGDASLKMDKSDAVSHTGNYTCEVTE LTREGETIIELKYRVVSWFSP
-
Molecular Weight
40 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
Osteoarthritis (OA) is a degenerative joint disease characterized by the breakdown of cartilage, leading to pain, stiffness, and reduced mobility. As the global population ages, OA prevalence continues to rise, making it a significant public health concern. Traditional treatment options typically focus on symptom management rather than addressing the underlying mechanisms of cartilage degeneration. Recent advancements in regenerative medicine have spurred interest in the use of recombinant proteins as potential therapeutic agents to promote cartilage repair and regeneration. These proteins, which can include growth factors and signaling molecules, aim to enhance chondrocyte survival, stimulate extracellular matrix production, and modulate inflammatory responses within the joint environment. Research has shown that OA-specific recombinant proteins can not only alleviate symptoms but also play a crucial role in restoring joint function by targeting the biological processes involved in cartilage homeostasis. This has led to a growing body of studies exploring the efficacy of these recombinant proteins in preclinical and clinical settings. The focus is now on optimizing their delivery mechanisms and understanding their interactions within the biological milieu of the joint, raising the potential for developing novel therapeutic strategies that can significantly improve the quality of life for individuals suffering from OA. As the understanding of the molecular and cellular pathways involved in OA deepens, the development and application of these recombinant proteins are poised to revolutionize the management of this debilitating condition.











