Product Overview

Description

UBC9 belongs to the ubiquitin-conjugating enzyme family. It is a homologue of the E2 ubiquitin conjugating enzyme and participates in the covalent linking of SUMO-1 molecule to the target protein. This protein is present at a high level in spleen and lung. Moderate level of UBC9 is detected in kidney and liver. Low amount of UBC9 is observed in brain, whereas the 18 kDa band of UBC9 is barely visible or absent in heart and skeletal muscle. In heart and muscle extracts the UBC9 antibodies recognizes a 38 kDa protein band,but this band is not visible in extracts of other rat tissues.

Expression Host

Mammalian cells

Immunogen

UBC9 fusion protein Ag7885

Species Reactivity

Human; Mouse; Rat

Clonality

Monoclonal

Host Species

Mouse

Isotype

IgG2a

Clone Number

CBP2639

Applications

FC; IHC; WB; ELISA

Application Notes

IHC : 1:20-1:200; WB : 1:500-1:1000

Research Areas

Growth and Development

Conjugation

Unconjugated

Product Properties

Form

Liquid

Formulation

PBS, 0.1% sodium azide and 50% glycerol pH 7.3.

Preservatives

Yes

Concentration

1200 μg/ml

Purification

Antigen affinity purification

Purity

>95%, as determined by SDS-PAGE

Shipping

The product is shipped at 4°C. Upon receipt, store it immediately at the temperature recommended below.

Storage

Store at -20°C. Stable for one year after shipment.

Research Use Only

For research use only, not for diagnostic or therapeutic use.

Target

UBC9

Official Name

UBC9

Full Name

Ubiquitin-conjugating enzyme E2I (UBC9 homolog, yeast)

Alternative Names

C358B7.1; E2; UBE2I; P18; SUMO conjugating enzyme UBC9; SUMO protein ligase; UBC9; UBCE9

Gene ID

7329(Human); 100044900(Mouse); 25573(Rat)

Uniprot ID

P63279(Human); P63280(Mouse); P63281(Rat)

References

1. Sohn, S. Y., & Hearing, P. (2019). Mechanism of Adenovirus E4-ORF3-Mediated SUMO Modifications. Mbio, 10(1). 2. Wang, T., Xu, W., Qin, M., Yang, Y., Bao, P., Shen, F.,... & Xu, J. (2016). Pathogenic mutations in the valosin-containing protein/p97 (VCP) N-domain inhibit the SUMOylation of VCP and lead to impaired stress response. Journal of Biological Chemistry, 291(27), 14373-14384. 3. Ye, X., Pan, T., Wang, D., Fang, L., Ma, J., Zhu, X.,... & Li, K. (2018). Foot-and-mouth disease virus counteracts on internal ribosome entry site suppression by G3BP1 and inhibits G3BP1-mediated stress granule assembly via post-translational mechanisms. Frontiers in immunology, 9, 1142.

Publications