Analytical Data
-
Gene name
COL5a2
- Application
-
Alternative Names
COL5-A2; Collagen Alpha-2(V)chain; AB Collagen
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P05997
-
Expression Region
Cys82~Glu308
-
Molecular Weight
52kDa
-
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
Collagen type V alpha 2 (COL5A2) is a crucial component of the extracellular matrix, playing a significant role in the structural integrity and mechanical properties of various tissues. It is a member of the fibrillar collagen family and is primarily involved in the regulation of collagen fibril formation and organization. Mutations in the COL5A2 gene have been implicated in various connective tissue disorders, most notably Ehlers-Danlos syndrome (EDS), which is characterized by hyper-flexibility of joints, skin hyper-elasticity, and a predisposition to joint dislocations and cardiovascular complications. Understanding the function and mechanisms of COL5A2 is essential for elucidating the pathogenesis of these conditions and for the development of targeted therapies. Recombinant COL5A2 protein has emerged as a valuable tool in research for studying collagen assembly, stability, and interactions within the extracellular matrix. Furthermore, it has potential applications in tissue engineering and regenerative medicine, where harnessing the unique properties of collagen can lead to breakthroughs in repairing damaged tissues and understanding cellular responses to the extracellular environment. The ongoing research into COL5A2 not only enhances our knowledge of connective tissue biology but also offers promise for therapeutic innovations in treating collagen-related disorders.
