GDC-H | H protein of glycine decarboxylase complex (GDC)
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GDC-H | H protein of glycine decarboxylase complex (GDC)

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Cat: PA00931
Size: 200 µg
Host: Rabbit
Clonality: Polyclonal
Confirmed reactivity: Arabidopsis thaliana, Cyanthobasis fruticulosa, Petrosimonia nigdeensis, Petunia hybrida cv. Mitchell, Portulaca grandiflora, Salsola grandis, Salsola tragus, Spinacia oleracea, Triticum aestivum, Vicia faba
Datasheet:

Product Info

Immunogen
purified GDC-H protein from Spinacia oleracea
Host
Rabbit
Clonality
Polyclonal
Purity
Total IgG. Protein G purified in PBS pH 7.4.
Format
Lyophilized
Reconstitution
For reconstitution add 200 µl of sterile water
Storage
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.
Application
Tissue printing (TP), Western blot (WB)
Recommended dilution
1 : 5 000 (TP), (WB)
Expected | apparent MW
16 kDa

Reactivity

Confirmed reactivity
Arabidopsis thaliana, Cyanthobasis fruticulosa, Petrosimonia nigdeensis, Petunia hybrida cv. Mitchell, Portulaca grandiflora, Salsola grandis, Salsola tragus, Spinacia oleracea, Triticum aestivum, Vicia faba
Predicted reactivity
higher plants
Not reactive in
No confirmed exceptions from predicted reactivity are currently known

Additional information

Cellular [compartment marker] of mitochondrial matrix,This antibody can be used on total cell extract of Arabidopsis thaliana.

Description

Glycine decarboxylase complex (GDC) is abundant in the mitochondrial matrix of C3 leaves and plays a role in photorespiration carbon recovery. GDC enzymes can account for up to 50% of matrix proteins and are responsible for the most prominent metabolic activity in light leaf mitochondria, photorespiration. GDC is a multienzyme complex composed of four enzymes, P-, H-, T- and L-protein, which is responsible for converting glycine produced by peroxisomes into serine in mitochondria during the photorespiratory cycle. The h protein plays a key role as a mobile substrate that travels back and forth between the other subunits, allowing its lipoic acid "arm" to access the active sites of the other three components.

For research use only, not for clinical use.