HERPUD1 Human

HERPUD1 Human Recombinant
Cat. No.
BT14825
Source
Escherichia Coli.
Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.
HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
HERPUD1 is a multi-pass membrane protein located within the endoplasmic reticulum, where it plays a crucial role in the quality control system. Characterized by its N-terminal ubiquitin-like domain, HERPUD1 is highly expressed in the brain. This protein, also known as ER-associated degradation (ERAD), participates in the ubiquitin-dependent degradation of misfolded proteins within the endoplasmic reticulum.
Description
Recombinant HERPUD1, produced in E. coli, is a single polypeptide chain consisting of 286 amino acids (residues 1-263) with a molecular weight of 31.6 kDa. This protein features a 23 amino acid His-tag fused to its N-terminus and undergoes purification using proprietary chromatographic techniques.
Physical Appearance
Clear solution, sterile-filtered.
Formulation
The provided HERPUD1 solution has a concentration of 0.5 mg/ml and is prepared in a phosphate-buffered saline (pH 7.4) solution containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing of the solution should be avoided.
Purity
SDS-PAGE analysis indicates a purity exceeding 85.0%.
Synonyms
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.

Product Science Overview

Gene and Protein Structure

The HERPUD1 gene is located on chromosome 16 in humans . The protein encoded by this gene contains an N-terminal ubiquitin-like domain, which is essential for its interaction with the ER-associated degradation (ERAD) system . This system is responsible for the ubiquitination and subsequent degradation of misfolded proteins in the ER .

Function and Mechanism

HERPUD1 is an early marker of ER stress and is involved in the unfolded protein response (UPR) . The UPR aims to restore normal function by halting protein translation, degrading misfolded proteins, and activating signaling pathways that lead to increased production of molecular chaperones involved in protein folding . HERPUD1 is also implicated in the regulation of calcium ion homeostasis within the ER .

Role in Disease

HERPUD1 has been associated with several diseases, including hereditary breast ovarian cancer syndrome . Its role in tumorigenesis, particularly in ovarian cancer, has been studied, revealing that HERPUD1 promotes cancer cell survival by sustaining autophagy . This suggests that HERPUD1 could be a potential target for therapeutic interventions in cancer treatment .

Recombinant HERPUD1

Recombinant HERPUD1 refers to the protein produced through recombinant DNA technology, which allows for the expression of the HERPUD1 protein in various host cells. This technology is crucial for studying the protein’s function and for developing potential therapeutic applications.

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THE BIOTEK
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