Recombinant Human Gastrin-Releasing Peptide (GRP) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-10945P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Gastrin-Releasing Peptide (GRP) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-10945P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Gastrin-Releasing Peptide (GRP) Protein (GST) is produced by our Yeast expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P07492
Target Symbol GRP
Synonyms BN; Bombesin; GRP; GRP-10; GRP_HUMAN; GRP10; Neuromedin-C; NeuromedinC; Pre progastrin releasing peptide; PreproGRP; ProGRP
Species Homo sapiens (Human)
Expression System Yeast
Tag N-GST
Target Protein Sequence STGESSSVSERGSLKQQLREYIRWEEAARNLLGLIEAKENRNHQPPQPKALGNQQPSWDSEDSSNFKD
Expression Range 54-121aa
Protein Length Partial
Mol. Weight 35.1 kDa
Research Area Signal Transduction
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Stimulates the release of gastrin and other gastrointestinal hormones. Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior. Contributes primarily to nonhistaminergic itch sensation. Contributes to long-term fear memory, but not normal spatial memory. Contributes to the regulation of food intake.
Subcellular Location Secreted. Cytoplasmic vesicle, secretory vesicle lumen.
Protein Families Bombesin/neuromedin-B/ranatensin family
Database References

Gene Functions References

  1. A panel of three tumor markers CYFRA 21.1, HE4 and ProGRP may play a role for discriminating LC from benign lung disease and subtyping as SCLC. PMID: 29729229
  2. Pro-GRP is sensitive for SCLC diagnosis. Since high marker levels are related to high disease burden, pro-GRP may have a negative prognostic significance. Follow-up studies are required to define its role in clinical practice in monitoring responses to treatment and early relapses PMID: 28967066
  3. Altogether, these data show that humanized anti-progastrin antibodies might represent a potential new treatment for K-RAS-mutated colorectal patients, for which there is a crucial unmet medical need PMID: 28600477
  4. Both TRPV1 and GRP are implied in midbrain physiology of importance to neurological and neuropsychiatric disorders. PMID: 27762319
  5. GRP/GRP-R signaling activation contributes to castration-resistant prostate cancer progression PMID: 27542219
  6. progastrin expression may be predictive of aggressive tumour behaviour in patients with colorectal cancer. PMID: 28432443
  7. Thus the combination of favourable in vitro and in vivo properties renders BA1 as more potential antagonist bombesin-peptide for targeting GRP-receptor positive tumor. These properties are encouraging to carry out further experiments for non-invasive receptor targeting potential diagnostinc and therapeutic agent for tumors. PMID: 28088445
  8. serum level not a biomarker in small cell lung cancer PMID: 29145241
  9. pro-gastrin releasing peptide has a role in promoting the cell proliferation and progression in small cell lung cancer PMID: 27639644
  10. Our results suggest that, similar to what happens in neutrophils, gastrin-releasing peptide is a migratory, rather than a proliferative, stimulus, for non-small cell lung carcinoma cells, indicating a putative role for gastrin-releasing peptide and gastrin-releasing peptide receptor in metastasis PMID: 28351312
  11. Serum Pro-GRP was promising biomarker for SCLC diagnosis. PMID: 28230031
  12. High proGRP expression is associated with poor response to chemotherapy in small cell lung cancer. PMID: 26886220
  13. CEA, NSE, CA125 and pro-GRP could serve as biomarkers for SCLC, and CEA and CYFRA21-1 could serve as biomarkers for NSCLC. Pro-GRP, CA125 and CEA were related to the clinical stages of lung cancer PMID: 26560853
  14. Data show that serum neuron-specific enolase, cytokeratin 19 fragment 21-1, pro-gastrin-releasing peptide, squamous cell carcinoma antigen, tissue inhibitor of metalloproteinase-1, and human epididymis protein 4 are not associated with brain metastases. PMID: 26730601
  15. Our results suggest that progastrin inhibits the acquisition of a M2-phenotype in human macrophages. PMID: 24901518
  16. No association of 16 GRP and 7 GRPR variants were found with agoraphobia with/without panic disorder. PMID: 24912045
  17. the role of autophagy in the degradation of gastrin-releasing peptide and subsequent inhibition of angiogenesis PMID: 24108003
  18. High serum proGRP levels are associated with small-cell lung cancer. PMID: 24375395
  19. The Gastrin-releasing peptide(GRP)triggers the growth of HepG2 cells through blocking the ER stress-mediated pathway. PMID: 23379566
  20. GRP silencing decreases anchorage-independent growth, inhibits cell migration and neuroblastoma cell-mediated angiogenesis. PMID: 24039782
  21. GRP-expressing C and A delta fibers that coexpress SP or CGRP makes these neurons pruriceptors. PMID: 23615431
  22. The levels of GRP were upregulated in cells treated with HGF in a dose-dependent manner. HGF-induced expression of Ets-1 and IL-8 was increased more by GRP treatment. PMID: 23924923
  23. inhibits the process of autophagy in vascular endothelial cells, thereby increasing endothelial cell proliferation and tubule formation PMID: 23608754
  24. GRP serum level is higher in patients with pruritus in patients with atopic dermatitis. PMID: 23353988
  25. Tonic stretch of human myometrium increases contractility and stimulates the expression of a known smooth muscle stimulatory agonist, GRP. GRP receptor antagonists attenuate the effect of stretch. PMID: 22411014
  26. Data indicate that progastrin-releasing peptide (proGRP) assays with both time-resolved immunofluorometric assay (TR-IFMA) and Advanced Life Science Institute (ALSI) ELISA showed good clinical validity. PMID: 22399443
  27. Percent changes in serum ProGRP showed better correlation to the sum of the tumor diameters (SOD) and prognostic impact than that of NSE. PMID: 22300752
  28. Results describe the mRNA expression of CRABP1, RERG, and GRP in pituitary adenomas. PMID: 21270509
  29. nonamidated peptides derived from the C terminus of pro-GRP are expressed in significant quantities in colorectal cancer cell lines PMID: 22202166
  30. proGRP is a complementary tumour marker for prognosis and treatment monitoring in patients with neuroendocrine tumour PMID: 21415235
  31. serum-positive non-small-cell lung cancers may have neuroendocrine differentiation PMID: 21529988
  32. Progastrin-releasing peptide cab be used as a marker for quality control in clinical sample processing and storage. PMID: 22261454
  33. Abrogating GRP/GRPR signaling specifically down-regulates HP1(Hsbeta) expression and inhibiting GRPR signaling, or ablating HP1(Hsbeta) expression, increases colon cancer cell invasiveness in vitro. PMID: 21281799
  34. Gastrin-releasing peptide is elevated in prostate neoplasm patients undergoing androgen deprivation therapy and may be involved in the initiation of hormonal escape prostate neoplasms. PMID: 20945407
  35. GRP promotes the growth of HepG2 cells through interaction with GRPR co-expressed in tumor cells, and subsequently activates MAPK/ERK1/2 via EGFR-independent mechanisms. PMID: 20596631
  36. Data indicate that various serum proGRP fragments are promising tools for future investigations on the relationship between fragment distribution and diagnosis and prognosis. PMID: 19907206
  37. GRP/GRP-R play a transient and non-critical role in intestinal development PMID: 11960700
  38. mRNA transcripts are expressed in tumor cells of patients with small cell lung cancer PMID: 12474049
  39. ProGRP is a valuable tumour marker for the detection and monitoring of small cell lung cancer (SCLC) and a good tool for discriminating non-small cell lung cancer (NSCLC) versus SCLC PMID: 12820318
  40. results show that Pro-GRP may be a potential tumor marker for small cell lung carcinoma PMID: 12820319
  41. Mitogenic effects of GRP in head and neck squamous cells are mediated by activation of the epidermal growth factor receptor. PMID: 13679857
  42. GRP is over-expressed in esophageal squamous cell carcinoma, and its over-expression may play a role in such carcinoma development and growth PMID: 14764456
  43. Measuring serum levels in lung cancer patients may be useful in drug therapy monitoring. PMID: 15638385
  44. GRP is a new angiogenic peptide and that its inhibition offers an attractive tool to reduce tumor burden. PMID: 15750618
  45. An increase in GRP binding capacity, as a result of GRP-R overexpression, down-regulates PTEN expression. Inhibition of the tumor suppressor gene PTEN may be an important regulatory mechanism involved in GRP-induced cell proliferation in neuroblastomas. PMID: 15849504
  46. BN/GRP and substance P are involved together with cytokines in the neuroimmunomodulation that occurs in the arthritic joint. PMID: 15899028
  47. results show that TACE undergoes phosphorylation that regulates release of amphiregulin upon GRP treatment; a signaling cascade of GRP-Src-PI3-K-PDK1-TACE-amphiregulin-EGFR with multiple points of interaction, translocation & phosphorylation is suggested PMID: 16641105
  48. First evidence is provided that the calcium-ion/calcineurin/NFAT-linked pathway is involved in bombesin-mediated induction of Cox-2, a gene that promotes colon carcinoma invasiveness. PMID: 16909108
  49. GRP upregulation of ICAM-1 via FAK promotes tumor cell motility and attachment to the extracellular matrix. PMID: 16920698
  50. BN/GRP is produced by non-neuronal cells in the synovial tissue in rheumatoid and osteoarthritis PMID: 18289674

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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