HSP90B1 Human, HEK

Heat Shock Protein 90kDa Beta (GRP94) Member 1 Human Recombinant, HEK
Cat. No.
BT17576
Source
HEK 293.
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
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
Prospec'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 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asp22-Glu798) containing a total of 789 amino acids, having a calculated molecular mass of 90.9kDa. HSP90B1 is fused to a 2 aa N-terminal linker, a 4 aa C-terminal linker and a 6 aa His tag at C-Terminus.

Product Specs

Introduction
HSP90B1, a member of the Hsp90 family, is an abundant molecular chaperone found in the endoplasmic reticulum (ER) lumen. It plays a crucial role in maintaining protein homeostasis within the secretory pathway. Additionally, HSP90B1 is involved in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway in antigen-presenting cells. This protein is essential for signal transduction, protein folding, protein degradation, and morphological development. HSP90B1 interacts with numerous cochaperones and participates in the folding of newly synthesized proteins and the stabilization and refolding of denatured proteins following stress. Notably, HSP90B1 exhibits high expression levels throughout the entire cell cycle in human gastric carcinoma BGC-823 cells.
Description
Recombinant HSP90B1, produced in HEK cells, is a single, glycosylated polypeptide chain with a molecular weight of 90.9 kDa. The protein sequence comprises amino acids Asp22 to Glu798, totaling 789 amino acids. It includes a 2-amino acid N-terminal linker, a 4-amino acid C-terminal linker, and a 6-histidine tag at the C-terminus.
Physical Appearance
White, lyophilized powder after filtration.
Formulation
HSP90B1 undergoes filtration (0.4 µm) and lyophilization in a solution of phosphate-buffered saline (PBS) at pH 8.0, containing 1% (w/v) sucrose and 4% (w/v) mannitol.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5 mg/ml. Allow the pellet to dissolve completely. Note: HSP90B1 is not sterile. Before using it in cell culture, ensure to filter the product through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to prevent repeated freeze-thaw cycles. The reconstituted protein can be stored at 4°C for a limited duration.
Purity
The purity is determined to be greater than 90.0% using 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
HEK 293.
Amino Acid Sequence
ASDDEVDVDG TVEEDLGKSR EGSRTDDEVV QREEEAIQLD GLNASQIREL REKSEKFAFQ AEVNRMMKLI INSLYKNKEI FLRELISNAS DALDKIRLIS LTDENALSGN EELTVKIKCD KEKNLLHVTD TGVGMTREEL VKNLGTIAKS GTSEFLNKMT EAQEDGQSTS ELIGQFGVGF YSAFLVADKV IVTSKHNNDT QHIWESDSNE FSVIADPRGN TLGRGTTITL VLKEEASDYL ELDTIKNLVK KYSQFINFPI YVWSSKTETV EEPMEEEEAA KEEKEESDDE AAVEEEEEEK KPKTKKVEKT VWDWELMNDI KPIWQRPSKE VEEDEYKAFY KSFSKESDDP MAYIHFTAEG EVTFKSILFV PTSAPRGLFD EYGSKKSDYI KLYVRRVFIT DDFHDMMPKY LNFVKGVVDS DDLPLNVSRE TLQQHKLLKV IRKKLVRKTL DMIKKIADDK YNDTFWKEFG TNIKLGVIED HSNRTRLAKL LRFQSSHHPT DITSLDQYVE RMKEKQDKIY FMAGSSRKEA ESSPFVERLL KKGYEVIYLT EPVDEYCIQA LPEFDGKRFQ NVAKEGVKFD ESEKTKESRE AVEKEFEPLL NWMKDKALKD KIEKAVVSQR LTESPCALVA SQYGWSGNME RIMKAQAYQT GKDISTNYYA SQKKTFEINP RHPLIRDMLR RIKEDEDDKT VLDLAVVLFE TATLRSGYLL PDTKAYGDRI ERMLRLSLNI DPDAKVEEEP EEEPEETAED TTEDTEQDED EEMDVGTDEE ETAKESTAE G PKLHHHHHH.

Product Science Overview

Structure and Localization

HSP90B1 is primarily localized in the endoplasmic reticulum (ER), where it is involved in the processing and transport of secreted proteins . The protein has ATPase activity, which is essential for its function as a molecular chaperone . It is also found in melanosomes and has been associated with various cellular components, including the cytosol, endocytic vesicle lumen, and extracellular matrix .

Function

The primary function of HSP90B1 is to assist in the proper folding of proteins within the ER. It is particularly important for the folding of Toll-like receptors and integrins, which are crucial for immune responses . HSP90B1 also plays a role in the endoplasmic reticulum-associated degradation (ERAD) pathway, which is responsible for the degradation of misfolded proteins . Additionally, it has been implicated in the regulation of both innate and adaptive immunity .

Clinical Significance

HSP90B1 is associated with various pathogenic states, including tumor formation . Its expression is linked to several diseases, such as Pelizaeus-Merzbacher-Like Disease and Nemaline Myopathy 9 . The protein’s role in immune regulation and protein folding makes it a potential target for therapeutic interventions in diseases related to protein misfolding and immune dysfunction.

Recombinant Production

The recombinant form of HSP90B1, produced in Human Embryonic Kidney (HEK) cells, is used for research purposes. This recombinant protein retains the functional properties of the native protein and is utilized in studies related to protein folding, immune responses, and disease mechanisms.

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