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AB156061

Recombinant Human HIP2/LIG protein

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Recombinant Human HIP2/LIG protein is a Human Full Length protein, in the 1 to 200 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, WB.

View Alternative Names

HIP2, LIG, UBE2K, Ubiquitin-conjugating enzyme E2 K, E2 ubiquitin-conjugating enzyme K, Huntingtin-interacting protein 2, Ubiquitin carrier protein, Ubiquitin-conjugating enzyme E2-25 kDa, Ubiquitin-protein ligase, HIP-2, Ubiquitin-conjugating enzyme E2(25K), Ubiquitin-conjugating enzyme E2-25K

1 Images
SDS-PAGE - Recombinant Human HIP2/LIG protein (AB156061)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human HIP2/LIG protein (AB156061)

SDS-PAGE analysis of ab156061.

Key facts

Purity

>95% Densitometry

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, WB

applications

Biologically active

No

Accession

P61086

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7 Preservative: 1.02% Imidazole Constituents: 25% Glycerol (glycerin, glycerine), 1.76% Sodium chloride, 0.82% Sodium phosphate, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF

storage-buffer

Reactivity data

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

Product details

This product was previously labelled as HIP2

Sequence info

[{"sequence":"MANIAVQRIKREFKEVLKSEETSKNQIKVDLVDENFTELRGEIAGPPDTPYEGGRYQLEIKIPETYPFNPPKVRFITKIWHPNISSVTGAICLDILKDQWAAAMTLRTVLLSLQALLAAAEPDDPQDAVVANQYKQNPEMFKQTARLWAHVYAGAPVSSPEYTKKIENLCAMGFDRNAVIVALSSKSWDVETATELLLSN","proteinLength":"Full Length","predictedMolecularWeight":"25 kDa","actualMolecularWeight":null,"aminoAcidEnd":200,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P61086","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

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

Supplementary information

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

HIP2 also known as LIG or Ubiquitin-Conjugating Enzyme E2 K (UBE2K) functions as an E2 ubiquitin-conjugating enzyme. It has a molecular mass of approximately 24 kDa. This protein plays an important role in the ubiquitination process where it transfers ubiquitin molecules to substrate proteins labeling them for degradation. HIP2 is expressed across various tissues in the human body indicating its widespread importance in cellular activities. It works alongside ubiquitin ligases (E3s) to ensure accurate tagging of proteins facilitating their removal by the proteasome.
Biological function summary

The function of HIP2 extends to protein homeostasis essential for maintaining cellular integrity. As part of the ubiquitin-proteasome system it ensures the elimination of damaged or excess proteins effectively preventing cellular stress or dysfunction. HIP2 operates within a complex that includes E1 enzymes and various E3 ligases highlighting its collaborative nature in protein turnover. The protein activity helps regulate cell cycle progression DNA repair and signal transduction ensuring normal cell function and adaptation to environmental changes.

Pathways

HIP2 is most involved in the ubiquitin-proteasome pathway and is linked to protein catabolism. It collaborates with key proteins like UBE2C and UBE2D which participate in tagging proteins for degradation. The coordination with these proteins demonstrates HIP2's role in managing protein levels in cells having implications in the cell's response to damage and stress. Additionally HIP2 intersects with pathways associated with cell cycle regulation allowing cells to maintain orderly division and prevent the accumulation of aberrant proteins.

HIP2 is significantly associated with neurodegenerative conditions and cancers. Aberrant HIP2 function can affect pathways controlled by proteins like p53 resulting in insufficient protein degradation that contributes to neuronal accumulation in disorders such as Alzheimer's disease. Moreover HIP2 dysregulation has links to oncogenic processes connecting to proteins like cyclins which are critical regulators in various cancers. Investigation into HIP2's function offers insights into potential therapeutic targets for these severe conditions with ongoing research focusing on modulating its activity to manage or prevent disease progression.

Specifications

Form

Liquid

Additional notes

Purity is lot specific. Please contact our technical Support team for details.

General info

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Post-translational modifications

Sumoylation at Lys-14 impairs catalytic activity.

Product protocols

Target data

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
See full target information UBE2K

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