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AB164040

Recombinant Human RNF128/GRAIL protein (GST tag N-Terminus)

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Recombinant Human RNF128/GRAIL protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 428 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

E3 ubiquitin-protein ligase RNF128, Gene related to anergy in lymphocytes protein, RING finger protein 128, RING-type E3 ubiquitin transferase RNF128, GRAIL, RNF128

1 Images
SDS-PAGE - Recombinant Human RNF128/GRAIL protein (GST tag N-Terminus) (AB164040)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human RNF128/GRAIL protein (GST tag N-Terminus) (AB164040)

ab164040 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q8TEB7

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product was previously labelled as RNF128.
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Sequence info

[{"sequence":"MGPPPGAGVSCRGGCGFSRLLAWCFLLALSPQAPGSRGAEAVWTAYLNVSWRVPHTGVNRTVWELSEEGVYGQDSPLEPVAGVLVPPDGPGALNACNPHTNFTVPTVWGSTVQVSWLALIQRGGGCTFADKIHLAYERGASGAVIFNFPGTRNEVIPMSHPGAVDIVAIMIGNLKGTKILQSIQRGIQVTMVIEVGKKHGPWVNHYSIFFVSVSFFIITAATVGYFIFYSARRLRNARAQSRKQRQLKADAKKAIGRLQLRTLKQGDKEIGPDGDSCAVCIELYKPNDLVRILTCNHIFHKTCVDPWLLEHRTCPMCKCDILKALGIEVDVEDGSVSLQVPVSNEISNSASSHEEDNRSETASSGYASVQGTDEPPLEEHVQSTNESLQLVNHEANSVAVDVIPHVDNPTFEEDETPNQETAVREIKS","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":428,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q8TEB7","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RNF128 also known as Gene Related to Anergy in Lymphocytes (GRAIL) is an E3 ubiquitin ligase with a molecular mass of approximately 44 kDa. This protein plays a mechanical role in tagging proteins with ubiquitin marking them for degradation by the proteasome. RNF128 is expressed in various tissues but it shows significant expression in immune cells particularly T cells. The protein contributes to regulating protein stability which is essential for maintaining cellular homeostasis and proper immune function.
Biological function summary

RNF128 is integral in regulating T cell anergy a state where T cells become unresponsive to antigenic stimulation. This protein helps maintain immune tolerance by suppressing excessive T cell responses preventing autoimmune reactions. RNF128 performs its biological function by being part of a complex that modulates signaling pathways involved in lymphocyte activation. Its expression and activity are modulated during immune responses regulating immune cell function and maintaining balance within the immune system.

Pathways

RNF128 is significantly involved in the ubiquitin-proteasome pathway impacting signal transduction and transcription processes. This protein is relevant in pathways related to immune tolerance particularly in controlling T cell receptor signaling. RNF128 interacts with other proteins like CD28 and CTLA-4 which are critical to T cell co-stimulatory and inhibitory pathways respectively. This interaction ensures the fine-tuning of immune responses preventing inappropriate activation that can lead to pathological states.

RNF128 has associations with autoimmune diseases and cancer. Its role in regulating immune tolerance links it to conditions like systemic lupus erythematosus where dysregulation can lead to an exaggerated immune response. Additionally RNF128's involvement in modulating T cell inactivity makes it relevant in certain cancers where immune evasion plays a critical role in disease progression. Through these conditions RNF128 remains connected with proteins like PD-1 which are involved in inhibitory pathways important for maintaining immune homeostasis.
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Specifications

Form

Liquid

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General info

Function

E3 ubiquitin-protein ligase that catalyzes 'Lys-27', 'Lys-48'- or 'Lys-63'-linked polyubiquitin chains formation and plays a role in different biological processes such as modulation of immune response, cytoskeletal dynamics or protein homeostasis. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production (PubMed : 12705856). Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytoskeletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse (PubMed : 22016387). Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. Plays a positive role in innate immune response by promoting 'Lys-63'-linked ubiquitination of TBK1 after RNA- or DNA-virus infection (PubMed : 27776110). Regulates alveolar macrophage activation and neutrophil infiltration by interacting with TLR4, targeting it for degradation, and inhibiting NF-kappa-B activation, hence decreasing pro-inflammatory cytokines (PubMed : 37344492). Negatively regulates the IL-3/STAT5 signaling pathway by facilitating 'Lys-27'-linked polyubiquitination of IL3RA leading to its degradation via lysosomal pathway (PubMed : 38702781). Directly regulates the N-glycosylation process in the endoplasmic reticulum by targeting the glycosyl-transferase RPN1 for ubiquitination and degradation (PubMed : 39567208). Other substrates targeted for degradation by RNF128 include transmembrane proteins CD40L, CD83 or the tetraspanin CD151 (PubMed : 18713730, PubMed : 19542455).

Post-translational modifications

Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination.

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Product protocols

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Target data

E3 ubiquitin-protein ligase that catalyzes 'Lys-27', 'Lys-48'- or 'Lys-63'-linked polyubiquitin chains formation and plays a role in different biological processes such as modulation of immune response, cytoskeletal dynamics or protein homeostasis. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production (PubMed : 12705856). Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytoskeletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse (PubMed : 22016387). Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. Plays a positive role in innate immune response by promoting 'Lys-63'-linked ubiquitination of TBK1 after RNA- or DNA-virus infection (PubMed : 27776110). Regulates alveolar macrophage activation and neutrophil infiltration by interacting with TLR4, targeting it for degradation, and inhibiting NF-kappa-B activation, hence decreasing pro-inflammatory cytokines (PubMed : 37344492). Negatively regulates the IL-3/STAT5 signaling pathway by facilitating 'Lys-27'-linked polyubiquitination of IL3RA leading to its degradation via lysosomal pathway (PubMed : 38702781). Directly regulates the N-glycosylation process in the endoplasmic reticulum by targeting the glycosyl-transferase RPN1 for ubiquitination and degradation (PubMed : 39567208). Other substrates targeted for degradation by RNF128 include transmembrane proteins CD40L, CD83 or the tetraspanin CD151 (PubMed : 18713730, PubMed : 19542455).
See full target information E3 ubiquitin-protein ligase RNF128
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