Rabbit Polyclonal DDRGK1 antibody. Suitable for IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human DDRGK1 aa 1-100.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine)
IHC-P | |
---|---|
Human | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/50.00000 - 1/200.00000 | Notes Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Component of the UFM1 ribosome E3 ligase (UREL) complex, a multiprotein complex that catalyzes ufmylation of endoplasmic reticulum-docked proteins (PubMed:30626644, PubMed:32160526, PubMed:35753586, PubMed:36121123, PubMed:36543799, PubMed:37595036, PubMed:37795761, PubMed:38383785, PubMed:38383789). The UREL complex plays a key role in ribosome recycling by mediating mono-ufmylation of the RPL26/uL24 subunit of the 60S ribosome following ribosome dissociation: ufmylation weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane (PubMed:38383785, PubMed:38383789). Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either take place after normal termination of translation or after ribosome stalling during cotranslational translocation at the endoplasmic reticulum (PubMed:37595036, PubMed:38383785, PubMed:38383789). Within the UREL complex, DDRGK1 tethers the complex to the endoplasmic reticulum membrane to restrict its activity to endoplasmic reticulum-docked ribosomes and acts as an ufmylation 'reader': following RPL26/uL24 ufmylation, DDRGK1 specifically binds to ufmylated RPL26/uL24 via its UFIM motif, resulting in stable association between the 60S ribosome and the UREL complex, followed by dissociation of the 60S ribosome subunit from the endoplasmic reticulum membrane (PubMed:36121123, PubMed:37595036, PubMed:38383785, PubMed:38383789). The UREL complex is also involved in reticulophagy in response to endoplasmic reticulum stress by promoting ufmylation of proteins such as CYB5R3 and RPN1, thereby promoting lysosomal degradation of ufmylated proteins (PubMed:32160526, PubMed:36543799). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) by regulating ERN1/IRE1-alpha stability (PubMed:28128204, PubMed:32160526). Acts as a regulator of immunity by promoting differentiation of B-cells into plasma cells: acts by promoting expansion of the endoplasmic reticulum and regulating the unfolded protein response (UPR) (By similarity). May also be required for TRIP4 ufmylation (PubMed:25219498). May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIA, the inhibitor of NF-kappa-B (PubMed:23675531). Plays a role in cartilage development through SOX9, inhibiting the ubiquitin-mediated proteasomal degradation of this transcriptional regulator (PubMed:28263186). Required for stabilization and ufmylation of ATG9A (By similarity).
C20orf116, UFBP1, DDRGK1, DDRGK domain-containing protein 1, Dashurin, UFM1-binding and PCI domain-containing protein 1
Rabbit Polyclonal DDRGK1 antibody. Suitable for IHC-P and reacts with Human samples. Immunogen corresponding to Recombinant Fragment Protein within Human DDRGK1 aa 1-100.
pH: 7.2
Preservative: 0.02% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine)
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DDRGK1 also known as DNA-damage responsive RING finger protein is a protein weighing approximately 34 kDa. It performs mechanical tasks related to protein modification and degradation. This protein has involvement in the ubiquitination process. DDRGK1 appears in several tissues with expression observed in the brain liver heart and skeletal muscle. Its presence in these diverse tissues suggests it plays many roles in cellular function.
DDRGK1 functions as a partner in complexes involved in protein quality control. It associates with the ubiquitin-proteasome system affecting protein turnover and stability. By controlling degradation DDRGK1 ensures cellular homeostasis and response to stress. Its role in protein homeostasis highlights the importance of regulation in cellular functions related to stress responses and damage repair mechanisms.
DDRGK1 is important in the ER-associated degradation (ERAD) pathway where it helps manage the degradation of misfolded proteins. This pathway links DDRGK1 to proteins like UBQLN2 and HRD1 which are significant in maintaining endoplasmic reticulum homeostasis. Additionally DDRGK1 modulates signaling pathways connected to inflammation underlining its role in broader cellular signaling mechanisms.
DDRGK1 links to neurodegenerative diseases and cancer. Abnormal DDRGK1 levels correlate with pathologies like amyotrophic lateral sclerosis (ALS) where its interaction with UBQLN2 plays a role. In cancer DDRGK1's involvement in protein degradation pathways impacts tumor growth and progression. These connections highlight the protein's significance in maintaining cellular health and the consequences of its dysregulation.
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Paraffin-embedded human adrenal gland tissue stained for DDRGK1 using ab251704 at 1/50 dilution in immunohistochemical analysis.
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