Recombinant Human Collagen IV alpha 6 protein (GST tag N-Terminus)
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(1 Publication)
Recombinant Human Collagen IV alpha 6 protein (GST tag N-Terminus) is a Human Full Length protein, in the 23 to 73 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Collagen alpha-6(IV) chain, COL4A6
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Collagen IV alpha 6 protein (GST tag N-Terminus) (AB158158)
ab158158 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
As part of the collagen IV network COL4A6 contributes to the formation of the heterotrimeric type IV collagen molecules. These trimers are composed of three alpha chains that associate to form a complex structure necessary for providing mechanical support and filtration functions in the basement membrane. The involvement of COL4A6 in these processes highlights its important role in tissue morphogenesis and maintenance.
Pathways
The function of COL4A6 integrates into major signaling cascades like the integrin-mediated signaling pathway and the extracellular matrix (ECM) remodeling pathway. Within these pathways COL4A6 collaborates with other collagen IV proteins such as COL4A1 and COL4A5 to interact with integrins. These interactions are critical for signal transduction processes that regulate cell adhesion migration and differentiation thereby maintaining tissue architecture.
Specifications
Form
Liquid
General info
Function
Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Sequence similarities
Belongs to the type IV collagen family.
Post-translational modifications
Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.. Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.. The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.
Target data
Publications (1)
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International journal of molecular sciences 22: PubMed34948383
2021
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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