Recombinant Mouse Endoplasmin (Hsp90b1)

Code CSB-YP010814MO
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Source Yeast
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Code CSB-EP010814MO
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Source E.coli
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Code CSB-EP010814MO-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP010814MO
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Source Baculovirus
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Code CSB-MP010814MO
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Hsp90b1
Uniprot No.
Alternative Names
Hsp90b1; Grp94; Tra-1; Tra1Endoplasmin; 94 kDa glucose-regulated protein; GRP-94; Endoplasmic reticulum resident protein 99; ERp99; Heat shock protein 90 kDa beta member 1; Polymorphic tumor rejection antigen 1; Tumor rejection antigen gp96
Species
Mus musculus (Mouse)
Expression Region
22-802
Target Protein Sequence
DDEVDVDGT VEEDLGKSRE GSRTDDEVVQ REEEAIQLDG LNASQIRELR EKSEKFAFQA EVNRMMKLII NSLYKNKEIF LRELISNASD ALDKIRLISL TDENALAGNE ELTVKIKCDK EKNLLHVTDT GVGMTREELV KNLGTIAKSG TSEFLNKMTE AQEDGQSTSE LIGQFGVGFY SAFLVADKVI VTSKHNNDTQ HIWESDSNEF SVIADPRGNT LGRGTTITLV LKEEASDYLE LDTIKNLVRK YSQFINFPIY VWSSKTETVE EPLEEDEAAK EEKEESDDEA AVEEEEEEKK PKTKKVEKTV WDWELMNDIK PIWQRPSKEV EEDEYKAFYK SFSKESDDPM AYIHFTAEGE VTFKSILFVP TSAPRGLFDE YGSKKSDYIK LYVRRVFITD DFHDMMPKYL NFVKGVVDSD DLPLNVSRET LQQHKLLKVI RKKLVRKTLD MIKKIADEKY NDTFWKEFGT NIKLGVIEDH SNRTRLAKLL RFQSSHHSTD ITSLDQYVER MKEKQDKIYF MAGSSRKEAE SSPFVERLLK KGYEVIYLTE PVDEYCIQAL PEFDGKRFQN VAKEGVKFDE SEKTKESREA TEKEFEPLLN WMKDKALKDK IEKAVVSQRL TESPCALVAS QYGWSGNMER IMKAQAYQTG KDISTNYYAS QKKTFEINPR HPLIRDMLRR IKEDEDDKTV MDLAVVLFET ATLRSGYLLP DTKAYGDRIE RMLRLSLNID PEAQVEEEPE EEPEDTSEDA EDSEQDEGEE MDAGTEEEEE ETEKESTEKD EL
Protein Length
Full Length of Mature Protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
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℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function
Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10.
Gene References into Functions
  1. Study demonstrated that the lack of gp96 in both the human monocytic cell line MM6 and in macrophages from LysMcre-gp96 floxed mice neither leads to a complete loss of TLR 2 expression nor to a complete loss of TLR-induced signaling, but is associated with an impaired phosphorylation of ERK and p38. These results reveal for the first time a crucial role for gp96 in the regulation of ERK and p38 kinases. PMID: 29447283
  2. GRP94 Knock-out mice exhibits impaired glucose tolerance. GRP94 is an essential regulator of pancreatic beta-cell development, mass, and function. PMID: 29272356
  3. These data demonstrate the essential role of the gp96-TLR interaction in priming T cell immunity and provide further molecular basis for the coupling of gp96-mediated innate with adaptive immunity. PMID: 27183126
  4. Heat-shock protein gp96 enhances T cell responses and protective potential to BCG vaccine. PMID: 27417661
  5. binding of PCSK9 to GRP94 protects LDLR from degradation likely by preventing early binding of PCSK9 to LDLR PMID: 26628375
  6. mgp96 could be a potential therapeutic target for ER-alpha36-overexpressing breast cancer. PMID: 26396174
  7. These data indicate that macrophage gp96 is essential for protective immunity during Gram-negative pneumonia PMID: 26365983
  8. gp96 participates in the generation of natural Treg cells, which might be involved in the control of liver regeneration in the periphery PMID: 25693689
  9. These studies imply GRP78, but not GRP94, is required for mammary gland development. PMID: 24953136
  10. GRP94 deficiency in the liver led to injury, LPC expansion, increased proliferation, activation of oncogenic signaling, progressive repopulation of GRP94-positive hepatocytes and HCC development in aged mice. PMID: 25220589
  11. GP96 serves as an essential chaperone for the cell-surface protein glycoprotein A repetitions predominant (GARP), which is a docking receptor for latent membrane-associated TGF-beta (mLTGF-beta). PMID: 25607841
  12. this work uncovered the essential role of gp96 in regulating melanogenesis. PMID: 24024552
  13. Deletion of CD24 impairs development of heat shock protein gp96-driven autoimmune disease through expansion of myeloid-derived suppressor cells. PMID: 24808359
  14. This study uncovers novel and unique roles of GRP94 in regulating hematopoietic stem cell proliferation. PMID: 23859598
  15. gp96 is an endoplasmic reticulum heat shock protein that serves as a morphogenetic and immunoregulatory factor in syngeneic pregnancy PMID: 23553495
  16. GRP94 is a novel regulator of cell adhesion, liver homeostasis, and tumorigenesis. PMID: 24027047
  17. gp96 is an immune chaperone with a role in macrophage-involved inflammatory colon tumorigenesis PMID: 24322981
  18. Induction of regulatory T cells by high-dose gp96 suppresses murine liver immune hyperactivation. PMID: 23874845
  19. gp96 is the major interaction partner of YFAK copolymer in RAW264.7 cells, confirmed by analysis of gp96-deficient cell lines and primary antigen-presenting cells. PMID: 23740953
  20. Data indicate that the dimerization of integrin alphaL and beta2 is highly dependent on gp96. PMID: 23671277
  21. grp94 plays a role in chaperoning LRP6-MesD in coordinating intestinal homeostasis, placing canonical Wnt-signaling pathway under the direct regulation of the general protein quality control machinery in the endoplasmic reticulum. PMID: 23572575
  22. shows that muscles rely on GRP94 primarily to support local production of IGFs, a pool that is necessary for normal muscle growth PMID: 22649033
  23. TLR7 requires a proteolytic cleavage by AEP to generate a C-terminal fragment competent for signaling. PMID: 22876182
  24. Our study revealed a remarkable biochemical event of gp96 silencing in murine but not human basophils, highlighting the need for caution in using mouse models to infer the function of basophils in human immune response. PMID: 22724016
  25. Chaperone gp96-independent inhibition of endotoxin response by chaperone-based peptide inhibitors. PMID: 22532561
  26. Gp96 is required for cell surface expression of at least four members of the extended LDL receptor family, as well CD180/Ly86 and most integrins and TLRs. PMID: 22292497
  27. The results reveal that EC-K1 exploits surface-expressed gp96 in PMNs to prevent oxidative burst for the onset of neonatal meningitis. PMID: 22109526
  28. We provide genetic and biochemical evidence to definitively demonstrate that a C-terminal loop structure, formed by residues 652-678, is the critical region of client binding domain for both TLRs and integrins. PMID: 22223641
  29. The nuclear localization signal sequence-dependent Grp94 kinase in the cell lysate is identical with CK2. PMID: 21739154
  30. Data indicate that grp94 is critically required for the assembly of GPIb-IX complex in platelets and megakaryocytes. grp94 Knockout mice exhibit thrombocytopenia, prolonged bleeding time, and giant platelets (indistinguishable from human BSS). PMID: 21576699
  31. GRP94 as a novel cell intrinsic factor required to maintain the interaction of hematopoietic stem cell with their niche, and thus regulate their physiology PMID: 21647226
  32. Hsp90b1 is involved in unique and specific aspects of the first mitosis, which brings together the maternal and paternal genomes on a single spindle. PMID: 21358806
  33. Data suggest that CNPY3 interacts with the ATP-sensitive conformation of gp96 to promote substrate loading. Our study has thus established CNPY3 as a TLR-specific cochaperone for gp96. PMID: 20865800
  34. Existing controversies regarding CD91 function in GRP94 surface binding and endocytic uptake establish fluid-phase uptake as a prominent mechanism for internalization of GRP94-peptide complexes into cross-presentation pathways. PMID: 21048103
  35. surface translocation of gp96 has a role in systemic lupus erythematosus PMID: 20352117
  36. GRP94 may play an important role in specific adult organ homeostasis and function. PMID: 20520781
  37. Gp96 and calreticulin chaperone the majority of antigenic peptides in the endoplasmic reticulum before exiting in association with class I histocompatibility antigen heavy chains and beta 2-microglobulin as a trimolecular complex. PMID: 20410492
  38. Data suggest that the major effect of GRP94 on muscle differentiation is mediated by its regulation of IGF production. PMID: 19914304
  39. findings define gp96 as the only known molecular chaperone to specifically regulate T- and B-cell development PMID: 19965672
  40. Our results provide new insights into the mechanisms of gp96-mediated balance between regulatory and responder T cells PMID: 19839010
  41. Cell surface targeting induces dendritic cell maturation and antitumor immunity PMID: 11739487
  42. Heat shock protein gp96 activates the release of nitric oxide by antigen presenting cells. PMID: 11884472
  43. examination of the binding of several peptides to recombinant GRP94 and study the regulation and site of peptide binding PMID: 12189140
  44. The identity of a 99- to 105-kDa protein on lipopolysaccharide-stimulated B cell surface is revealed as gp96 and its function as a Th2-specific costimulatory molecule is established. PMID: 12244140
  45. Gp96 (murine) binds to human neutrophils and monocytes and stimulates effector functions, increases phagocytosis activity, and increases IL-8 production. PMID: 12446445
  46. GRP94-elicited tumor suppression can occur independent of the GRP94 tissue of origin and suggest a primary role for GRP4 natural adjuvant function in antitumor immune responses. PMID: 12461080
  47. elicits ERK activation in murine macrophages PMID: 12805368
  48. Chronic stimulation of dendritic cellss by gp96 is a pathway to initiate spontaneous autoimmune diseases. PMID: 14668429
  49. Administration of syngeneic GRP94/gp96- or GRP94/gp96-N-terminal domain-secreting KBALB fibroblasts to BALB/c mice stimulates CD11b+ and CD11c+ antigen presenting cell function and promotes bystander activation of CD4+ T cell Th1 cytokine production. PMID: 15034032
  50. Orientia tsutsugamushi down-regulated gp96 in murine peritoneal cells PMID: 15107540

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Subcellular Location
Endoplasmic reticulum lumen. Sarcoplasmic reticulum lumen. Melanosome.
Protein Families
Heat shock protein 90 family
Database Links
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