HSPH1 Human

Heat Shock Protein 105 Human Recombinant
Cat. No.
BT19132
Source
Escherichia Coli.
Synonyms
HSPH1, Heat Shock protein 105kDa, 110kDa protein 1, Heat shock 110 kDa protein, HSP110, HSP105A, Antigen NY-CO-25, HSP105, HSP105A, HSP105B, KIAA0201, NY-CO-25, DKFZp686M05240.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Recombinant HSPH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 894 amino acids and having a molecular mass of 100.9kDa. HSP105 Alpha is fused with a 36 a.a. His tag and purified by conventional chromatography techniques.

Product Specs

Introduction
HSPH1 analysis serves as both an indicator and diagnostic tool for problematic lesions. It plays a crucial role in the endoplasmic reticulum (ER) stress response by chaperoning interactions between GRP78, GSK3, and itself. In the absence of HSP105, cell death triggered by ER stress follows a non-caspase-3-dependent pathway. Notably, HSPH1 exhibits elevated expression levels in a wide array of human tumors. As a mammalian representative of the HSP105/110 family, a distinct subgroup within the HSP70 family, HSP105 exists in two isoforms: alpha and beta. Hsp105a forms complexes with Hsp70/Hsc70 in vivo, exerting a negative regulatory effect on their chaperone activity both in vitro and in vivo.
Description
Recombinant HSPH1, expressed in E.Coli, is a single, non-glycosylated polypeptide chain comprising 894 amino acids. With a molecular weight of 100.9kDa, HSP105 Alpha is engineered to include a 36 amino acid His tag and is purified using standard chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The HSP105 protein solution is formulated in 20mM Tris-HCl buffer at pH 8.0 with 50mM NaCl.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
Purity exceeds 90.0% as assessed by SDS-PAGE analysis.
Synonyms
HSPH1, Heat Shock protein 105kDa, 110kDa protein 1, Heat shock 110 kDa protein, HSP110, HSP105A, Antigen NY-CO-25, HSP105, HSP105A, HSP105B, KIAA0201, NY-CO-25, DKFZp686M05240.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSVV GLDVGSQSCY IAVARAGGIE TIANEFSDRC TPSVISFGSK NRTIGVAAKN QQITHANNTV SNFKRFHGRA FNDPFIQKEK ENLSYDLVPL KNGGVGIKVM YMGEEHLFSV EQITAMLLTK LKETAENSLK KPVTDCVISV PSFFTDAERR SVLDAAQIVG LNCLRLMNDM TAVALNYGIY KQDLPSLDEK PRIVVFVDMG HSAFQVSACA FNKGKLKVLG TAFDPFLGGK NFDEKLVEHF CAEFKTKYKL DAKSKIRALL RLYQECEKLK KLMSSNSTDL PLNIECFMND KDVSGKMNRS QFEELCAELL QKIEVPLYSL LEQTHLKVED VSAVEIVGGA TRIPAVKERI AKFFGKDIST TLNADEAVAR GCALQCAILS PAFKVREFSV TDAVPFPISL IWNHDSEDTE GVHEVFSRNH AAPFSKVLTF LRRGPFELEA FYSDPQGVPY PEAKIGRFVV QNVSAQKDGE KSRVKVKVRV NTHGIFTIST ASMVEKVPTE
ENEMSSEADM ECLNQRPPEN PDTDKNVQQD NSEAGTQPQV QTDAQQTSQS PPSPELTSEE NKIPDADKAN EKKVDQPPEA KKPKIKVVNV ELPIEANLVW QLGKDLLNMY IETEGKMIMQ DKLEKERNDA KNAVEEYVYE FRDKLCGPYE KFICEQDHQN FLRLLTETED WLYEEGEDQA KQAYVDKLEE LMKIGTPVKV RFQEAEERPK MFEELGQRLQ HYAKIAADFR NKDEKYNHID ESEMKKVEKS VNEVMEWMNN VMNAQAKKSL DQDPVVRAQE IKTKIKELNN TCEPVVTQPK PKIESPKLER TPNGPNIDKK EEDLEDKNNF GAEPPHQNGE CYPNEKNSVN MDLD.

Product Science Overview

Introduction

Heat Shock Protein 105 (HSP105) is a mammalian stress protein that belongs to the HSP110 family. It is a 105-kDa protein that plays a crucial role in cellular stress responses. HSP105 is released by tissues in response to a wide variety of stresses, including infection, ischemia, heat stress, and tumors .

Discovery and Structure

HSP105 was discovered through serological analysis of recombinant cDNA expression libraries prepared from tumor cells (SEREX). This method helps define strongly immunogenic tumor antigens that elicit both cellular and humoral immunity . HSP105 consists of two components: the α-component, which is 105 kDa, and the β-component, a truncated form that is 90 kDa in size and is specifically induced by heat stress at 42°C .

Function and Mechanism

HSP105 functions as a molecular chaperone and apoptotic regulator. It prevents the aggregation of denatured proteins in cells under severe stress, where ATP levels decrease markedly . HSP105 also acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from these proteins and thereby triggering client/substrate protein release .

Expression and Clinical Significance

HSP105 is overexpressed in various internal malignancies, including colorectal carcinoma and melanoma cell lines . It is also overexpressed in squamous cell carcinoma and extramammary Paget disease but not in basal cell carcinoma . This overexpression makes HSP105 a potential target for immunotherapy. Studies have shown that HSP105 DNA vaccination can stimulate HSP105-specific tumor immunity, leading to tumor regression .

Industrial and Research Applications

Recombinant HSP105 is used in various research applications to study its role in stress responses and its potential as a therapeutic target. It is also used in the development of vaccines and immunotherapies for cancers that overexpress HSP105 .

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THE BIOTEK
THE BioTek is a global biotech company offering highly purified proteins for research in cancer, apoptosis, development, endocrinology, immunology, neuroscience, proteases, and stem cells.
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