HSP90B1 Human
Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant
Cat. No.
BT17500
Source
Escherichia Coli.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
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
HSP90B1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 819 amino acids (22-803 a.a.) and having a molecular mass of 94.4 kDa.
HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
HSP90B1 is expressed with a 36 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
HSP90B1, also known as GRP94, is a chaperone protein primarily located in the endoplasmic reticulum (ER). It plays a crucial role in protein quality control by assisting in the folding and assembly of newly synthesized proteins and preventing the aggregation of misfolded proteins. HSP90B1 is highly expressed in gastric cancer cells and is involved in tumor cell survival and proliferation. As part of the Hsp90 family, it participates in various cellular processes like signal transduction and stress response. This protein also interacts with the MHC class I antigen processing pathway, influencing immune recognition of cancer cells.
Description
This product consists of the recombinant human HSP90B1 protein, produced in E. coli. The protein sequence spans amino acids 22 to 803, excluding the signal peptide, and includes a 36-amino acid Histidine tag at the N-terminus for purification purposes. The final product is a single, non-glycosylated polypeptide chain with a molecular weight of 94.4 kDa. Purification is achieved using proprietary chromatographic methods, resulting in a highly pure protein suitable for various research applications.
Physical Appearance
The product is a clear and colorless solution after sterile filtration.
Formulation
The HSP90B1 protein is supplied in a solution containing 20mM Tris-HCl (pH 8.0), 1mM EDTA, 0.1M NaCl, 1mM DTT, and 10% glycerol. The protein concentration is 1mg/ml.
Stability
For short-term storage (up to 4 weeks), keep the product refrigerated at 4°C. For extended storage, freeze the product at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. To preserve protein integrity, minimize repeated freeze-thaw cycles.
Purity
The purity of the HSP90B1 protein is greater than 90%, as determined by SDS-PAGE analysis.
Synonyms
ECGP, GP96, TRA1, GRP94, HSP90B1, Endoplasmin, Heat shock protein 90 kDa beta member 1, 94 kDa glucose-regulated protein, gp96 homolog, Tumor rejection antigen 1.
Source
Escherichia Coli.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDDE VDVDGTVEED LGKSREGSRT DDEVVQREEE AIQLDGLNAS QIRELREKSE KFAFQAEVNR MMKLIINSLY KNKEIFLREL ISNASDALDK IRLISLTDEN ALSGNEELTV KIKCDKEKNL LHVTDTGVGM TREELVKNLG TIAKSGTSEF LNKMTEAQED GQSTSELIGQ FGVGFYSAFL VADKVIVTSK HNNDTQHIWE SDSNEFSVIA DPRGNTLGRG TTITLVLKEE ASDYLELDTI KNLVKKYSQF INFPIYVWSS KTETVEEPME EEEAAKEEKE ESDDEAAVEE EEEEKKPKTK KVEKTVWDWE LMNDIKPIWQ RPSKEVEEDE YKAFYKSFSK ESDDPMAYIH FTAEGEVTFK SILFVPTSAP RGLFDEYGSK KSDYIKLYVR RVFITDDFHD MMPKYLNFVK GVVDSDDLPL NVSRETLQQH KLLKVIRKKL VRKTLDMIKK IADDKYNDTF WKEFGTNIKL GVIEDHSNRT RLAKLLRFQS SHHPTDITSL DQYVERMKEK QDKIYFMAGS SRKEAESSPF VERLLKKGYE VIYLTEPVDE YCIQALPEFD GKRFQNVAKE GVKFDESEKT KESREAVEKE FEPLLNWMKD KALKDKIEKA VVSQRLTESP CALVASQYGW SGNMERIMKA QAYQTGKDIS TNYYASQKKT FEINPRHPLI RDMLRRIKED EDDKTVLDLA VVLFETATLR SGYLLPDTKA YGDRIERMLR LSLNIDPDAK VEEEPEEEPE ETAEDTTEDT EQDEDEEMDV GTDEEEETAK ESTAEKDEL.
Product Science Overview
Introduction
Heat Shock Protein 90kDa Beta (GRP94) Member 1, also known as HSP90B1, is a molecular chaperone that plays a crucial role in the folding, assembly, and stabilization of other proteins. It is a member of the heat shock protein 90 (HSP90) family and is predominantly found in the endoplasmic reticulum (ER) of cells. This protein is also referred to as endoplasmin, gp96, or ERp99 .
Gene and Protein Structure
The HSP90B1 gene is located on chromosome 12 in humans and encodes a protein that is approximately 803 amino acids long . The protein has several functional domains, including an ATPase domain that is essential for its chaperone activity. The ATPase activity of HSP90B1 is crucial for its function in protein folding and stabilization .
Function and Importance
HSP90B1 is involved in various cellular processes, including:
- Protein Folding: It assists in the proper folding of newly synthesized proteins and the refolding of misfolded proteins.
- Stress Response: It is upregulated in response to cellular stress, such as heat shock, and helps protect cells from stress-induced damage.
- Immune Response: HSP90B1 plays a role in the immune system by assisting in the presentation of antigens to immune cells, thereby facilitating the activation of the immune response .
Clinical Significance
HSP90B1 has been implicated in several diseases and pathological conditions:
- Cancer: Overexpression of HSP90B1 has been observed in various cancers, and it is thought to contribute to tumor progression by stabilizing oncogenic proteins.
- Neurodegenerative Diseases: Misfolding and aggregation of proteins are common features of neurodegenerative diseases, and HSP90B1 is involved in mitigating these effects by promoting proper protein folding .
Recombinant HSP90B1
Recombinant HSP90B1 is produced using recombinant DNA technology, where the HSP90B1 gene is cloned into an expression vector and introduced into a host cell, such as E. coli or yeast. The host cells then produce the HSP90B1 protein, which can be purified and used for various research and therapeutic applications .
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