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| Code | CSB-YP010827MO |
| Size | US$1916 |
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| Description |
The recombinant endoplasmic reticulum chaperone BiP (Hspa5) was produced as a fusion protein with an N-terminal 6xHis tag in the yeast cells. The encoding sequence contains 20-655aa of mouse Hspa5 protein. The purity of this full-length of mature Hspa5 protein reached up to 90% determined by SDS-PAGE. It migrated to a molecular mass band of 78-90 kDa on the gel. The slightly higher result is attributed to glycosylation. This recombinant Hspa5 protein can induce immune reactions in the immunized animals to thus get specific antibodies. Besides, it also may find uses in the tags and cell markers research area. Heat shock protein family A member 5 (Hspa5), also known as GRP78 or Bip, is a member of heat shock proteins (HSPs) that are involved in proper protein folding, assembly of multiprotein complexes, as well as protein transport and degradation. In response to the accumulation of misfolded proteins in the ER, endoplasmic chaperone protein Hspa5 dissociates from ATF6-IRE1-PERK complex and then translocates into the lumen of the ER. This process unlocks the activity of the signal transducers previously blocked, which leads to the activation of the UPR signaling pathways. Recently, surface HSPA5 has been reported to be a potential receptor of some viruses, including the novel SARS-CoV-2. |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Target Names | Hspa5 |
| Uniprot No. | P20029 |
| Research Area | Tags & Cell Markers |
| Alternative Names |
Hspa5; Grp78; Endoplasmic reticulum chaperone BiP; EC 3.6.4.10; 78 kDa glucose-regulated protein; GRP-78; Binding-immunoglobulin protein; BiP; Heat shock protein 70 family protein 5; HSP70 family protein 5; Heat shock protein family A member 5; Immunoglobulin heavy chain-binding protein
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| Species | Mus musculus (Mouse) |
| Source | Yeast |
| Expression Region | 20-655aa |
| Target Protein Sequence | EEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVCPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLGTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIERMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEEKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request. |
| Mol. Weight | 72.5kDa |
| Protein Length | Full Length of Mature Protein |
| Tag Info |
N-terminal 6xHis-tagged |
| Form |
Liquid or Lyophilized powder Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. |
| Buffer | If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0. |
| Reconstitution | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
| Troubleshooting and FAQs |
Protein FAQs |
| Storage Condition | Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. |
| Shelf Life | The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. |
| Lead Time | 3-7 business days |
| Notes | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
| Datasheet & COA | Please contact us to get it. |
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| Function |
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation.
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| Gene References into Functions |
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| Subcellular Location | Endoplasmic reticulum lumen. Melanosome. Cytoplasm. Cell surface. |
| Protein Families | Heat shock protein 70 family |
| Database Links |
KEGG: mmu:14828 STRING: 10090.ENSMUSP00000028222 UniGene: Mm.330160 |
