HSPA5 Human
Heat Shock 70kDa Protein 5 Human Recombinant
Cat. No.
BT17921
Source
Escherichia Coli.
Synonyms
BIP, MIF2, GRP78, FLJ26106, HSPA5, 78 kDa glucose-regulated protein, GRP 78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78.
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 Human HSPA5 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 640 amino acids (20-650 a.a.) and having a molecular mass of 71kDa.
HSPA5 human recombinant is fused to an 8 amino acid His Tag at C-terminus and purified by convential chromatogrpahy techniques.
Product Specs
Introduction
When glucose is deprived in Chinese hamster K12 cells, the production of glucose-regulated protein (GRP) is activated. HSPA5, also known as BiP and belonging to the HSP70 family, is involved in protein folding and assembly within the endoplasmic reticulum. It plays a crucial role in regulating protein transport throughout the cell. HSPA5, as a stress response protein, is induced by factors or situations that negatively impact endoplasmic reticulum function. It is essential for proper glycosylation, folding, maintaining cellular equilibrium, and preventing apoptosis. Studies have shown differential expression of HSPA5 in the dorsolateral prefrontal cortex of individuals with schizophrenia. Moreover, HSPA5 facilitates the entry of the hepatitis B virus large envelope protein into the mammalian endoplasmic reticulum during post-translational import. HSPA5 actively regulates various malignant characteristics, including cell growth, migration, and invasion.
Description
Recombinant Human HSPA5, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 640 amino acids (specifically, residues 20-650). It has a molecular weight of 71 kDa. This recombinant HSPA5 protein is engineered with an 8 amino acid His Tag at the C-terminus and is purified using standard chromatography methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HSPA5 protein solution is prepared in a buffer containing 20mM Tris-HCl at pH 8 and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), the protein should be kept at 4°C. For extended storage, it is recommended to freeze the protein at -20°C. Adding a carrier protein (either 0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing of the protein should be avoided.
Purity
The purity of the protein is determined to be greater than 90% using SDS-PAGE analysis.
Synonyms
BIP, MIF2, GRP78, FLJ26106, HSPA5, 78 kDa glucose-regulated protein, GRP 78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78.
Source
Escherichia Coli.
Amino Acid Sequence
MEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AELEHHHHHH.
Product Science Overview
Structure and Function
HSPA5 is a multifunctional protein that primarily resides in the endoplasmic reticulum (ER). It is involved in:
- Protein Folding: HSPA5 assists in the proper folding of nascent proteins and the refolding of misfolded proteins, ensuring they attain their functional conformations.
- Calcium Homeostasis: It helps maintain calcium balance within the ER, which is vital for various cellular functions.
- ER Stress Response: HSPA5 is a key regulator of the unfolded protein response (UPR), a cellular stress response related to the ER. It helps cells cope with the accumulation of misfolded proteins by enhancing the protein-folding capacity of the ER and reducing the load of newly synthesized proteins .
Role in Development and Disease
HSPA5 has been implicated in various physiological and pathological processes:
- Embryonic Development: HSPA5 is essential for early embryonic development. It mediates retinoic acid signaling, which is crucial for the formation of pronephros, an early kidney structure in vertebrates .
- Cancer: HSPA5 is often overexpressed in cancer cells, where it supports their survival and proliferation. It has been identified as a potential target for cancer therapy due to its role in protecting cells from stress-induced apoptosis .
- Neurodegenerative Diseases: Dysregulation of HSPA5 has been linked to neurodegenerative diseases such as Alzheimer’s and Parkinson’s, where it may contribute to the accumulation of misfolded proteins .
Recombinant HSPA5
Recombinant HSPA5 is produced using genetic engineering techniques, where the HSPA5 gene is cloned and expressed in a suitable host system, such as bacteria or yeast. This allows for the production of large quantities of the protein for research and therapeutic purposes.
- Research Applications: Recombinant HSPA5 is used in various research studies to understand its function and role in different cellular processes. It is also used to study the mechanisms of diseases where HSPA5 is implicated.
- Therapeutic Potential: Due to its role in protein folding and stress response, recombinant HSPA5 is being explored for potential therapeutic applications, including the treatment of diseases associated with protein misfolding and ER stress .
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