|Application ||WB, IHC-P, FC, E|
|Other Accession||P26516, Q3ZBD0|
|Calculated MW||37025 Da|
|Antigen Region||6-34 aa|
|Other Names||26S proteasome non-ATPase regulatory subunit 7, 26S proteasome regulatory subunit RPN8, 26S proteasome regulatory subunit S12, Mov34 protein homolog, Proteasome subunit p40, PSMD7, MOV34L|
|Target/Specificity||This PSMD7 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 6-34 amino acids from the N-terminal region of human PSMD7.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PSMD7 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
PSMD7 acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Dastani,Z., et.al., Eur. J. Hum. Genet. (2009) In press
Sanches,M., et.al., J. Mol. Biol. 370 (5), 846-855 (2007)
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