SIRT7 Antibody [J3K9] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:1000 IP1:30 IHC1:100

Application
WB, IP, IHC

Reactivity
Mouse, Rat, Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
44 kDa 45 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Datasheet & SDS

Biological Description

Specificity
SIRT7 Antibody [J3K9] detects endogenous levels of total SIRT7 protein.

Clone
J3K9

Synonym(s)
SIR2L7; SIRT7; NAD-dependent protein deacetylase sirtuin-7; NAD-dependent protein deacylase sirtuin-7; Regulatory protein SIR2 homolog 7; SIR2-like protein 7

Background
SIRT7 is an NAD±dependent deacetylase and Class III HDAC from the conserved sirtuin family SIRT1-7, primarily found in the nucleolus and highly expressed in hematopoietic cells such as myeloid progenitors. SIRT7 is essential for rRNA processing, chromatin silencing, and cellular transformation. It includes a unique N-terminal three-helical domain α1-α3 with arginines R30, R37, R64, R68, and R74 that mediate nucleosome and DNA engagement across the acidic patch and gyres, a flexible linker or hinge helix α2, and a catalytic core featuring DNA-binding loops such as H217, R218, K272-276, R289, and R290. F239 secures H3K36 in the active site, conferring deacylation specificity over H3K18. SIRT7 is recruited by Elk-4 to promoters, where it deacetylates H3K18 to repress transcription, maintains ribosomal biogenesis via RNA polymerase I, and facilitates DNA repair by deacetylating ATM for dephosphorylation. It shifts between tightly gripping DNA when targeting H3K36 and a relaxed, bent linker conformation when targeting H3K18. Overexpression of SIRT7 leads to global reduction of H3K18 acetylation, driving anchorage-independent growth, low-serum survival, cell-cycle entry, escape from contact inhibition, and tumorigenesis in xenograft models, while knockout impairs these transformed phenotypes. In cancer, SIRT7 amplification in prostate, lung, kidney, and pancreas correlates with poor prognosis through H3K18 hypoacetylation, and SIRT7 also promotes leukemia and lymphoma via 17q25 alterations and supports E1A-induced transformation.

Background

SIRT7 is an NAD±dependent deacetylase and Class III HDAC from the conserved sirtuin family SIRT1-7, primarily found in the nucleolus and highly expressed in hematopoietic cells such as myeloid progenitors. SIRT7 is essential for rRNA processing, chromatin silencing, and cellular transformation. It includes a unique N-terminal three-helical domain α1-α3 with arginines R30, R37, R64, R68, and R74 that mediate nucleosome and DNA engagement across the acidic patch and gyres, a flexible linker or hinge helix α2, and a catalytic core featuring DNA-binding loops such as H217, R218, K272-276, R289, and R290. F239 secures H3K36 in the active site, conferring deacylation specificity over H3K18. SIRT7 is recruited by Elk-4 to promoters, where it deacetylates H3K18 to repress transcription, maintains ribosomal biogenesis via RNA polymerase I, and facilitates DNA repair by deacetylating ATM for dephosphorylation. It shifts between tightly gripping DNA when targeting H3K36 and a relaxed, bent linker conformation when targeting H3K18. Overexpression of SIRT7 leads to global reduction of H3K18 acetylation, driving anchorage-independent growth, low-serum survival, cell-cycle entry, escape from contact inhibition, and tumorigenesis in xenograft models, while knockout impairs these transformed phenotypes. In cancer, SIRT7 amplification in prostate, lung, kidney, and pancreas correlates with poor prognosis through H3K18 hypoacetylation, and SIRT7 also promotes leukemia and lymphoma via 17q25 alterations and supports E1A-induced transformation.

References
https://pubmed.ncbi.nlm.nih.gov/39900593/ https://pubmed.ncbi.nlm.nih.gov/34129782/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%