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AB156061

Recombinant Human HIP2/LIG protein

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.

別名を表示する

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

Key facts

精製度

>95% Densitometry

発現系

Escherichia coli

タグ

His tag N-Terminus

アプリケーション

SDS-PAGE, WB

applications

生物活性

No

アクセッション番号

P61086

アニマルフリー

No

キャリアフリー

No

Human

バッファー組成

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>" } } }

製品の詳細

配列情報

[{"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"}]}]

出荷温度及び保存条件

出荷温度
Dry Ice
短期保存温度
-80°C
長期保存温度
-80°C
分注に関する情報
Upon delivery aliquot
保管に関する情報
Avoid freeze / thaw cycle
False

補足情報

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.

製品の性状

製品の状態

Liquid

補足情報

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

一般的な情報

機能

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.

配列の類似性

Belongs to the ubiquitin-conjugating enzyme family.

翻訳後修飾

Sumoylation at Lys-14 impairs catalytic activity.

製品プロトコール

ターゲットの情報

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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Recombinant Human HIP2/LIG protein

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